data_1FIU
# 
_entry.id   1FIU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1FIU         
NDB   PD0177       
RCSB  RCSB011623   
WWPDB D_1000011623 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1FIU 
_pdbx_database_status.recvd_initial_deposition_date   2000-08-07 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Deibert, M.'    1 
'Grazulis, S.'   2 
'Sasnauskas, G.' 3 
'Siksnys, V.'    4 
'Huber, R.'      5 
# 
_citation.id                        primary 
_citation.title                     'Structure of the tetrameric restriction endonuclease NgoMIV in complex with cleaved DNA.' 
_citation.journal_abbrev            Nat.Struct.Biol. 
_citation.journal_volume            7 
_citation.page_first                792 
_citation.page_last                 799 
_citation.year                      2000 
_citation.journal_id_ASTM           NSBIEW 
_citation.country                   US 
_citation.journal_id_ISSN           1072-8368 
_citation.journal_id_CSD            2024 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   10966652 
_citation.pdbx_database_id_DOI      10.1038/79032 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Deibert, M.'    1 
primary 'Grazulis, S.'   2 
primary 'Sasnauskas, G.' 3 
primary 'Siksnys, V.'    4 
primary 'Huber, R.'      5 
# 
_cell.entry_id           1FIU 
_cell.length_a           90.400 
_cell.length_b           91.130 
_cell.length_c           149.520 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1FIU 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     orthorhombic 
_symmetry.Int_Tables_number                19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     syn 
;DNA (5'-D(*TP*GP*CP*G)-3')
;
1206.829  4    ?        ? ? ? 
2 polymer     syn 
;DNA (5'-D(P*CP*CP*GP*GP*CP*GP*C)-3')
;
2099.387  4    ?        ? ? ? 
3 polymer     man 'TYPE II RESTRICTION ENZYME NGOMI'     31810.902 4    3.1.21.4 ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                        24.305    8    ?        ? ? ? 
5 non-polymer syn 'ACETIC ACID'                          60.052    4    ?        ? ? ? 
6 water       nat water                                  18.015    1279 ?        ? ? ? 
# 
_entity_name_com.entity_id   3 
_entity_name_com.name        'NGOMIV RESTRICTION ENDONUCLEASE, ENDONUCLEASE NGOMI, R.NGOMI' 
# 
_entity_name_sys.entity_id   3 
_entity_name_sys.name        E.C.3.1.21.4 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 polydeoxyribonucleotide no no '(DT)(DG)(DC)(DG)' TGCG E,F,G,H ? 
2 polydeoxyribonucleotide no no '(DC)(DC)(DG)(DG)(DC)(DG)(DC)' CCGGCGC I,J,K,L ? 
3 'polypeptide(L)'        no no 
;MQPLFTQERRIFHKKLLDGNILATNNRGVVSNADGSNTRSFNIAKGIADLLHSETVSERLPGQTSGNAFEAICSEFVQSA
FEKLQHIRPGDWNVKQVGSRNRLEIARYQQYAHLTALAKAAEENPELAAALGSDYTITPDIIVTRNLIADAEINRNEFLV
DENIATYASLRAGNGNMPLLHASISCKWTIRSDRAQNARSEGLNLVRNRKGRLPHIVVVTAEPTPSRISSIALGTGEIDC
VYHFALYELEQILQSLNYEDALDLFYIMVNGKRLKDISDLPLDLAV
;
;MQPLFTQERRIFHKKLLDGNILATNNRGVVSNADGSNTRSFNIAKGIADLLHSETVSERLPGQTSGNAFEAICSEFVQSA
FEKLQHIRPGDWNVKQVGSRNRLEIARYQQYAHLTALAKAAEENPELAAALGSDYTITPDIIVTRNLIADAEINRNEFLV
DENIATYASLRAGNGNMPLLHASISCKWTIRSDRAQNARSEGLNLVRNRKGRLPHIVVVTAEPTPSRISSIALGTGEIDC
VYHFALYELEQILQSLNYEDALDLFYIMVNGKRLKDISDLPLDLAV
;
A,B,C,D ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   DT  n 
1 2   DG  n 
1 3   DC  n 
1 4   DG  n 
2 1   DC  n 
2 2   DC  n 
2 3   DG  n 
2 4   DG  n 
2 5   DC  n 
2 6   DG  n 
2 7   DC  n 
3 1   MET n 
3 2   GLN n 
3 3   PRO n 
3 4   LEU n 
3 5   PHE n 
3 6   THR n 
3 7   GLN n 
3 8   GLU n 
3 9   ARG n 
3 10  ARG n 
3 11  ILE n 
3 12  PHE n 
3 13  HIS n 
3 14  LYS n 
3 15  LYS n 
3 16  LEU n 
3 17  LEU n 
3 18  ASP n 
3 19  GLY n 
3 20  ASN n 
3 21  ILE n 
3 22  LEU n 
3 23  ALA n 
3 24  THR n 
3 25  ASN n 
3 26  ASN n 
3 27  ARG n 
3 28  GLY n 
3 29  VAL n 
3 30  VAL n 
3 31  SER n 
3 32  ASN n 
3 33  ALA n 
3 34  ASP n 
3 35  GLY n 
3 36  SER n 
3 37  ASN n 
3 38  THR n 
3 39  ARG n 
3 40  SER n 
3 41  PHE n 
3 42  ASN n 
3 43  ILE n 
3 44  ALA n 
3 45  LYS n 
3 46  GLY n 
3 47  ILE n 
3 48  ALA n 
3 49  ASP n 
3 50  LEU n 
3 51  LEU n 
3 52  HIS n 
3 53  SER n 
3 54  GLU n 
3 55  THR n 
3 56  VAL n 
3 57  SER n 
3 58  GLU n 
3 59  ARG n 
3 60  LEU n 
3 61  PRO n 
3 62  GLY n 
3 63  GLN n 
3 64  THR n 
3 65  SER n 
3 66  GLY n 
3 67  ASN n 
3 68  ALA n 
3 69  PHE n 
3 70  GLU n 
3 71  ALA n 
3 72  ILE n 
3 73  CYS n 
3 74  SER n 
3 75  GLU n 
3 76  PHE n 
3 77  VAL n 
3 78  GLN n 
3 79  SER n 
3 80  ALA n 
3 81  PHE n 
3 82  GLU n 
3 83  LYS n 
3 84  LEU n 
3 85  GLN n 
3 86  HIS n 
3 87  ILE n 
3 88  ARG n 
3 89  PRO n 
3 90  GLY n 
3 91  ASP n 
3 92  TRP n 
3 93  ASN n 
3 94  VAL n 
3 95  LYS n 
3 96  GLN n 
3 97  VAL n 
3 98  GLY n 
3 99  SER n 
3 100 ARG n 
3 101 ASN n 
3 102 ARG n 
3 103 LEU n 
3 104 GLU n 
3 105 ILE n 
3 106 ALA n 
3 107 ARG n 
3 108 TYR n 
3 109 GLN n 
3 110 GLN n 
3 111 TYR n 
3 112 ALA n 
3 113 HIS n 
3 114 LEU n 
3 115 THR n 
3 116 ALA n 
3 117 LEU n 
3 118 ALA n 
3 119 LYS n 
3 120 ALA n 
3 121 ALA n 
3 122 GLU n 
3 123 GLU n 
3 124 ASN n 
3 125 PRO n 
3 126 GLU n 
3 127 LEU n 
3 128 ALA n 
3 129 ALA n 
3 130 ALA n 
3 131 LEU n 
3 132 GLY n 
3 133 SER n 
3 134 ASP n 
3 135 TYR n 
3 136 THR n 
3 137 ILE n 
3 138 THR n 
3 139 PRO n 
3 140 ASP n 
3 141 ILE n 
3 142 ILE n 
3 143 VAL n 
3 144 THR n 
3 145 ARG n 
3 146 ASN n 
3 147 LEU n 
3 148 ILE n 
3 149 ALA n 
3 150 ASP n 
3 151 ALA n 
3 152 GLU n 
3 153 ILE n 
3 154 ASN n 
3 155 ARG n 
3 156 ASN n 
3 157 GLU n 
3 158 PHE n 
3 159 LEU n 
3 160 VAL n 
3 161 ASP n 
3 162 GLU n 
3 163 ASN n 
3 164 ILE n 
3 165 ALA n 
3 166 THR n 
3 167 TYR n 
3 168 ALA n 
3 169 SER n 
3 170 LEU n 
3 171 ARG n 
3 172 ALA n 
3 173 GLY n 
3 174 ASN n 
3 175 GLY n 
3 176 ASN n 
3 177 MET n 
3 178 PRO n 
3 179 LEU n 
3 180 LEU n 
3 181 HIS n 
3 182 ALA n 
3 183 SER n 
3 184 ILE n 
3 185 SER n 
3 186 CYS n 
3 187 LYS n 
3 188 TRP n 
3 189 THR n 
3 190 ILE n 
3 191 ARG n 
3 192 SER n 
3 193 ASP n 
3 194 ARG n 
3 195 ALA n 
3 196 GLN n 
3 197 ASN n 
3 198 ALA n 
3 199 ARG n 
3 200 SER n 
3 201 GLU n 
3 202 GLY n 
3 203 LEU n 
3 204 ASN n 
3 205 LEU n 
3 206 VAL n 
3 207 ARG n 
3 208 ASN n 
3 209 ARG n 
3 210 LYS n 
3 211 GLY n 
3 212 ARG n 
3 213 LEU n 
3 214 PRO n 
3 215 HIS n 
3 216 ILE n 
3 217 VAL n 
3 218 VAL n 
3 219 VAL n 
3 220 THR n 
3 221 ALA n 
3 222 GLU n 
3 223 PRO n 
3 224 THR n 
3 225 PRO n 
3 226 SER n 
3 227 ARG n 
3 228 ILE n 
3 229 SER n 
3 230 SER n 
3 231 ILE n 
3 232 ALA n 
3 233 LEU n 
3 234 GLY n 
3 235 THR n 
3 236 GLY n 
3 237 GLU n 
3 238 ILE n 
3 239 ASP n 
3 240 CYS n 
3 241 VAL n 
3 242 TYR n 
3 243 HIS n 
3 244 PHE n 
3 245 ALA n 
3 246 LEU n 
3 247 TYR n 
3 248 GLU n 
3 249 LEU n 
3 250 GLU n 
3 251 GLN n 
3 252 ILE n 
3 253 LEU n 
3 254 GLN n 
3 255 SER n 
3 256 LEU n 
3 257 ASN n 
3 258 TYR n 
3 259 GLU n 
3 260 ASP n 
3 261 ALA n 
3 262 LEU n 
3 263 ASP n 
3 264 LEU n 
3 265 PHE n 
3 266 TYR n 
3 267 ILE n 
3 268 MET n 
3 269 VAL n 
3 270 ASN n 
3 271 GLY n 
3 272 LYS n 
3 273 ARG n 
3 274 LEU n 
3 275 LYS n 
3 276 ASP n 
3 277 ILE n 
3 278 SER n 
3 279 ASP n 
3 280 LEU n 
3 281 PRO n 
3 282 LEU n 
3 283 ASP n 
3 284 LEU n 
3 285 ALA n 
3 286 VAL n 
# 
_entity_src_gen.entity_id                          3 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     Neisseria 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Neisseria gonorrhoeae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     485 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PET15B 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_code 
_struct_ref.db_name 
_struct_ref.entity_id 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_db_isoform 
1 T2NM_NEIGO UNP 3 P31032 1 
;MNPLFTQERRIFHKKLLDGNILATNNRGVVSNADGSNTRSFNIAKGIADLLHSETVSERLPGQTSGNAFEAICSEFVQSA
FEKLQHIRPGDWNVKQVGSRNRLEIARYQQYAHLTALAKAAEENPELAAALGSDYTITPDIIVTRNLIADAEINRNEFLV
DENIATYASLRAGNGNMPLLHASISCKWTIRSDRAQNARSEGLNLVRNRKGRLPHIVVVTAEPTPSRISSIALGTGEIDC
VYHFALYELEQILQSLNYEDALDLFYIMVNGKRLKDISDLPLDLAV
;
? 
2 1FIU       PDB 1 1FIU   ? ? ? 
3 1FIU       PDB 2 1FIU   ? ? ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 1FIU A 1 ? 286 ? P31032 1 ? 286 ? 1 286 
2  1 1FIU B 1 ? 286 ? P31032 1 ? 286 ? 1 286 
3  1 1FIU C 1 ? 286 ? P31032 1 ? 286 ? 1 286 
4  1 1FIU D 1 ? 286 ? P31032 1 ? 286 ? 1 286 
5  2 1FIU E 1 ? 4   ? 1FIU   1 ? 4   ? 1 4   
6  3 1FIU I 1 ? 7   ? 1FIU   5 ? 11  ? 5 11  
7  2 1FIU F 1 ? 4   ? 1FIU   1 ? 4   ? 1 4   
8  3 1FIU J 1 ? 7   ? 1FIU   5 ? 11  ? 5 11  
9  2 1FIU G 1 ? 4   ? 1FIU   1 ? 4   ? 1 4   
10 3 1FIU K 1 ? 7   ? 1FIU   5 ? 11  ? 5 11  
11 2 1FIU H 1 ? 4   ? 1FIU   1 ? 4   ? 1 4   
12 3 1FIU L 1 ? 7   ? 1FIU   5 ? 11  ? 5 11  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 1FIU GLN A 2 ? UNP P31032 ASN 2 CONFLICT 2 1 
2 1FIU GLN B 2 ? UNP P31032 ASN 2 CONFLICT 2 2 
3 1FIU GLN C 2 ? UNP P31032 ASN 2 CONFLICT 2 3 
4 1FIU GLN D 2 ? UNP P31032 ASN 2 CONFLICT 2 4 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACY non-polymer         . 'ACETIC ACID'                        ? 'C2 H4 O2'        60.052  
ALA 'L-peptide linking' y ALANINE                              ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                             ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                           ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                      ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                             ? 'C3 H7 N O2 S'    121.158 
DC  'DNA linking'       y "2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE"  ? 'C9 H14 N3 O7 P'  307.197 
DG  'DNA linking'       y "2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE" ? 'C10 H14 N5 O7 P' 347.221 
DT  'DNA linking'       y "THYMIDINE-5'-MONOPHOSPHATE"         ? 'C10 H15 N2 O8 P' 322.208 
GLN 'L-peptide linking' y GLUTAMINE                            ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                      ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                              ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                            ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                           ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                              ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                               ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                           ? 'C5 H11 N O2 S'   149.211 
MG  non-polymer         . 'MAGNESIUM ION'                      ? 'Mg 2'            24.305  
PHE 'L-peptide linking' y PHENYLALANINE                        ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                              ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                               ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                            ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                           ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                             ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                               ? 'C5 H11 N O2'     117.146 
# 
_exptl.entry_id          1FIU 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   43.62 
_exptl_crystal.density_Matthews      2.18 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    'MES 100mM, MgCl2 200mM, MPD 25%, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
loop_
_exptl_crystal_grow_comp.crystal_id 
_exptl_crystal_grow_comp.id 
_exptl_crystal_grow_comp.sol_id 
_exptl_crystal_grow_comp.name 
_exptl_crystal_grow_comp.conc 
_exptl_crystal_grow_comp.volume 
_exptl_crystal_grow_comp.details 
1 1 1 MES   ? ? ? 
1 2 1 MgCl2 ? ? ? 
1 3 1 MPD   ? ? ? 
1 4 2 MES   ? ? ? 
1 5 2 MgCl2 ? ? ? 
1 6 2 MPD   ? ? ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           90 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1998-07-21 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0697 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'MPG/DESY, HAMBURG BEAMLINE BW6' 
_diffrn_source.pdbx_wavelength             1.0697 
_diffrn_source.pdbx_synchrotron_site       'MPG/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   BW6 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1FIU 
_reflns.observed_criterion_sigma_I   1. 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             17.26 
_reflns.d_resolution_high            1.6 
_reflns.number_obs                   160528 
_reflns.number_all                   162845 
_reflns.percent_possible_obs         98.6 
_reflns.pdbx_Rmerge_I_obs            0.0470000 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              15.7 
_reflns.R_free_details               ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.6 
_reflns_shell.d_res_low              ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.percent_possible_all   88.7 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1FIU 
_refine.ls_number_reflns_obs                     160612 
_refine.ls_number_reflns_all                     162845 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_d_res_low                             17.26 
_refine.ls_d_res_high                            1.6 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1729000 
_refine.ls_R_factor_R_free                       0.2038000 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 10 
_refine.ls_number_reflns_R_free                  16061 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8952 
_refine_hist.pdbx_number_atoms_nucleic_acid   892 
_refine_hist.pdbx_number_atoms_ligand         8 
_refine_hist.number_atoms_solvent             1295 
_refine_hist.number_atoms_total               11147 
_refine_hist.d_res_high                       1.6 
_refine_hist.d_res_low                        17.26 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_angle_deg 1.567 ? ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d    0.010 ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  1FIU 
_struct.title                     'TETRAMERIC RESTRICTION ENDONUCLEASE NGOMIV IN COMPLEX WITH CLEAVED DNA' 
_struct.pdbx_descriptor           'TYPE II RESTRICTION ENZYME NGOMI (E.C.3.1.21.4)/DNA COMPLEX' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1FIU 
_struct_keywords.pdbx_keywords   hydrolase/DNA 
_struct_keywords.text            
;PROTEIN-DNA COMPLEX, DOUBLE HELIX, RESTRICTION ENDONUCLEASE, RESTRICTION-MODIFICTION SYSTEMS, HYDROLASE, PHOSPHODIESTERASE, METAL ION, COMPLEX (ENDONUCLEASE-DNA), hydrolase-DNA COMPLEX
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 1 ? 
D  N N 2 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 1 ? 
H  N N 2 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 4 ? 
Q  N N 4 ? 
R  N N 5 ? 
S  N N 4 ? 
T  N N 5 ? 
U  N N 4 ? 
V  N N 5 ? 
W  N N 4 ? 
X  N N 5 ? 
Y  N N 6 ? 
Z  N N 6 ? 
AA N N 6 ? 
BA N N 6 ? 
CA N N 6 ? 
DA N N 6 ? 
EA N N 6 ? 
FA N N 6 ? 
GA N N 6 ? 
HA N N 6 ? 
IA N N 6 ? 
JA N N 6 ? 
# 
_struct_biol.id                    1 
_struct_biol.details               'The biological assembly is a tetramer' 
_struct_biol.pdbx_parent_biol_id   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  PRO I 3   ? GLY I 19  ? PRO A 3   GLY A 19  1 ? 17 
HELX_P HELX_P2  2  ASN I 37  ? LEU I 51  ? ASN A 37  LEU A 51  1 ? 15 
HELX_P HELX_P3  3  PRO I 61  ? GLU I 82  ? PRO A 61  GLU A 82  1 ? 22 
HELX_P HELX_P4  4  LYS I 83  ? GLN I 85  ? LYS A 83  GLN A 85  5 ? 3  
HELX_P HELX_P5  5  LEU I 103 ? TYR I 108 ? LEU A 103 TYR A 108 5 ? 6  
HELX_P HELX_P6  6  TYR I 108 ? TYR I 111 ? TYR A 108 TYR A 111 5 ? 4  
HELX_P HELX_P7  7  ALA I 112 ? GLU I 122 ? ALA A 112 GLU A 122 1 ? 11 
HELX_P HELX_P8  8  ASN I 124 ? GLY I 132 ? ASN A 124 GLY A 132 1 ? 9  
HELX_P HELX_P9  9  ALA I 149 ? ASN I 154 ? ALA A 149 ASN A 154 1 ? 6  
HELX_P HELX_P10 10 ASP I 193 ? ALA I 195 ? ASP A 193 ALA A 195 5 ? 3  
HELX_P HELX_P11 11 GLN I 196 ? ARG I 209 ? GLN A 196 ARG A 209 1 ? 14 
HELX_P HELX_P12 12 THR I 224 ? LEU I 233 ? THR A 224 LEU A 233 1 ? 10 
HELX_P HELX_P13 13 ALA I 245 ? ASN I 257 ? ALA A 245 ASN A 257 1 ? 13 
HELX_P HELX_P14 14 TYR I 258 ? GLY I 271 ? TYR A 258 GLY A 271 1 ? 14 
HELX_P HELX_P15 15 ASP I 279 ? LEU I 284 ? ASP A 279 LEU A 284 1 ? 6  
HELX_P HELX_P16 16 PRO J 3   ? GLY J 19  ? PRO B 3   GLY B 19  1 ? 17 
HELX_P HELX_P17 17 ASN J 37  ? LEU J 51  ? ASN B 37  LEU B 51  1 ? 15 
HELX_P HELX_P18 18 PRO J 61  ? LYS J 83  ? PRO B 61  LYS B 83  1 ? 23 
HELX_P HELX_P19 19 LEU J 103 ? TYR J 108 ? LEU B 103 TYR B 108 5 ? 6  
HELX_P HELX_P20 20 TYR J 108 ? TYR J 111 ? TYR B 108 TYR B 111 5 ? 4  
HELX_P HELX_P21 21 ALA J 112 ? ASN J 124 ? ALA B 112 ASN B 124 1 ? 13 
HELX_P HELX_P22 22 GLU J 126 ? GLY J 132 ? GLU B 126 GLY B 132 1 ? 7  
HELX_P HELX_P23 23 SER J 133 ? ILE J 137 ? SER B 133 ILE B 137 5 ? 5  
HELX_P HELX_P24 24 ALA J 149 ? ASN J 154 ? ALA B 149 ASN B 154 1 ? 6  
HELX_P HELX_P25 25 ASP J 193 ? ALA J 195 ? ASP B 193 ALA B 195 5 ? 3  
HELX_P HELX_P26 26 GLN J 196 ? ARG J 209 ? GLN B 196 ARG B 209 1 ? 14 
HELX_P HELX_P27 27 THR J 224 ? LEU J 233 ? THR B 224 LEU B 233 1 ? 10 
HELX_P HELX_P28 28 ALA J 245 ? LEU J 256 ? ALA B 245 LEU B 256 1 ? 12 
HELX_P HELX_P29 29 TYR J 258 ? GLY J 271 ? TYR B 258 GLY B 271 1 ? 14 
HELX_P HELX_P30 30 ASP J 279 ? LEU J 284 ? ASP B 279 LEU B 284 1 ? 6  
HELX_P HELX_P31 31 PRO K 3   ? GLY K 19  ? PRO C 3   GLY C 19  1 ? 17 
HELX_P HELX_P32 32 ASN K 37  ? LEU K 51  ? ASN C 37  LEU C 51  1 ? 15 
HELX_P HELX_P33 33 PRO K 61  ? LYS K 83  ? PRO C 61  LYS C 83  1 ? 23 
HELX_P HELX_P34 34 GLU K 104 ? TYR K 108 ? GLU C 104 TYR C 108 5 ? 5  
HELX_P HELX_P35 35 TYR K 108 ? TYR K 111 ? TYR C 108 TYR C 111 5 ? 4  
HELX_P HELX_P36 36 ALA K 112 ? ASN K 124 ? ALA C 112 ASN C 124 1 ? 13 
HELX_P HELX_P37 37 LEU K 127 ? GLY K 132 ? LEU C 127 GLY C 132 1 ? 6  
HELX_P HELX_P38 38 ALA K 149 ? ASN K 154 ? ALA C 149 ASN C 154 1 ? 6  
HELX_P HELX_P39 39 ASP K 193 ? ALA K 195 ? ASP C 193 ALA C 195 5 ? 3  
HELX_P HELX_P40 40 GLN K 196 ? ARG K 209 ? GLN C 196 ARG C 209 1 ? 14 
HELX_P HELX_P41 41 THR K 224 ? LEU K 233 ? THR C 224 LEU C 233 1 ? 10 
HELX_P HELX_P42 42 ALA K 245 ? ASN K 257 ? ALA C 245 ASN C 257 1 ? 13 
HELX_P HELX_P43 43 TYR K 258 ? GLY K 271 ? TYR C 258 GLY C 271 1 ? 14 
HELX_P HELX_P44 44 ASP K 279 ? LEU K 284 ? ASP C 279 LEU C 284 1 ? 6  
HELX_P HELX_P45 45 PRO L 3   ? GLY L 19  ? PRO D 3   GLY D 19  1 ? 17 
HELX_P HELX_P46 46 ASN L 37  ? LEU L 51  ? ASN D 37  LEU D 51  1 ? 15 
HELX_P HELX_P47 47 PRO L 61  ? GLU L 82  ? PRO D 61  GLU D 82  1 ? 22 
HELX_P HELX_P48 48 LYS L 83  ? GLN L 85  ? LYS D 83  GLN D 85  5 ? 3  
HELX_P HELX_P49 49 GLY L 98  ? ASN L 101 ? GLY D 98  ASN D 101 5 ? 4  
HELX_P HELX_P50 50 LEU L 103 ? TYR L 108 ? LEU D 103 TYR D 108 5 ? 6  
HELX_P HELX_P51 51 TYR L 108 ? ALA L 112 ? TYR D 108 ALA D 112 5 ? 5  
HELX_P HELX_P52 52 HIS L 113 ? ASN L 124 ? HIS D 113 ASN D 124 1 ? 12 
HELX_P HELX_P53 53 ASN L 124 ? GLY L 132 ? ASN D 124 GLY D 132 1 ? 9  
HELX_P HELX_P54 54 SER L 133 ? ILE L 137 ? SER D 133 ILE D 137 5 ? 5  
HELX_P HELX_P55 55 ALA L 149 ? ASN L 154 ? ALA D 149 ASN D 154 1 ? 6  
HELX_P HELX_P56 56 ASP L 193 ? ALA L 195 ? ASP D 193 ALA D 195 5 ? 3  
HELX_P HELX_P57 57 GLN L 196 ? ARG L 209 ? GLN D 196 ARG D 209 1 ? 14 
HELX_P HELX_P58 58 THR L 224 ? LEU L 233 ? THR D 224 LEU D 233 1 ? 10 
HELX_P HELX_P59 59 ALA L 245 ? ASN L 257 ? ALA D 245 ASN D 257 1 ? 13 
HELX_P HELX_P60 60 TYR L 258 ? GLY L 271 ? TYR D 258 GLY D 271 1 ? 14 
HELX_P HELX_P61 61 ASP L 279 ? LEU L 284 ? ASP D 279 LEU D 284 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1  metalc ? ? Q MG . MG ? ? ? 1_555 D  DC  1   OP2 ? ? A MG 5555 J DC  5    1_555 ? ? ? ? ? ? ?            2.140 ? 
metalc2  metalc ? ? Q MG . MG ? ? ? 1_555 I  CYS 186 O   ? ? A MG 5555 A CYS 186  1_555 ? ? ? ? ? ? ?            2.226 ? 
metalc3  metalc ? ? Q MG . MG ? ? ? 1_555 R  ACY .   O   ? ? A MG 5555 A ACY 2001 1_555 ? ? ? ? ? ? ?            2.307 ? 
metalc4  metalc ? ? Q MG . MG ? ? ? 1_555 BA HOH .   O   ? ? A MG 5555 J HOH 221  1_555 ? ? ? ? ? ? ?            2.159 ? 
metalc5  metalc ? ? Q MG . MG ? ? ? 1_555 GA HOH .   O   ? ? A MG 5555 A HOH 5564 1_555 ? ? ? ? ? ? ?            2.230 ? 
metalc6  metalc ? ? Q MG . MG ? ? ? 1_555 I  ASP 140 OD2 ? ? A MG 5555 A ASP 140  1_555 ? ? ? ? ? ? ?            2.180 ? 
metalc7  metalc ? ? S MG . MG ? ? ? 1_555 J  ASP 140 OD2 ? ? B MG 3333 B ASP 140  1_555 ? ? ? ? ? ? ?            2.197 ? 
metalc8  metalc ? ? S MG . MG ? ? ? 1_555 B  DC  1   OP2 ? ? B MG 3333 I DC  5    1_555 ? ? ? ? ? ? ?            2.158 ? 
metalc9  metalc ? ? S MG . MG ? ? ? 1_555 J  CYS 186 O   ? ? B MG 3333 B CYS 186  1_555 ? ? ? ? ? ? ?            2.226 ? 
metalc10 metalc ? ? S MG . MG ? ? ? 1_555 T  ACY .   OXT ? ? B MG 3333 B ACY 3002 1_555 ? ? ? ? ? ? ?            2.280 ? 
metalc11 metalc ? ? S MG . MG ? ? ? 1_555 Z  HOH .   O   ? ? B MG 3333 I HOH 57   1_555 ? ? ? ? ? ? ?            2.192 ? 
metalc12 metalc ? ? S MG . MG ? ? ? 1_555 HA HOH .   O   ? ? B MG 3333 B HOH 3390 1_555 ? ? ? ? ? ? ?            2.256 ? 
metalc13 metalc ? ? U MG . MG ? ? ? 1_555 V  ACY .   O   ? ? C MG 7777 C ACY 4003 1_555 ? ? ? ? ? ? ?            2.340 ? 
metalc14 metalc ? ? U MG . MG ? ? ? 1_555 F  DC  1   OP2 ? ? C MG 7777 K DC  5    1_555 ? ? ? ? ? ? ?            2.126 ? 
metalc15 metalc ? ? U MG . MG ? ? ? 1_555 IA HOH .   O   ? ? C MG 7777 C HOH 7781 1_555 ? ? ? ? ? ? ?            2.199 ? 
metalc16 metalc ? ? U MG . MG ? ? ? 1_555 K  CYS 186 O   ? ? C MG 7777 C CYS 186  1_555 ? ? ? ? ? ? ?            2.182 ? 
metalc17 metalc ? ? U MG . MG ? ? ? 1_555 K  ASP 140 OD2 ? ? C MG 7777 C ASP 140  1_555 ? ? ? ? ? ? ?            2.182 ? 
metalc18 metalc ? ? U MG . MG ? ? ? 1_555 DA HOH .   O   ? ? C MG 7777 K HOH 328  1_555 ? ? ? ? ? ? ?            2.214 ? 
metalc19 metalc ? ? W MG . MG ? ? ? 1_555 L  CYS 186 O   ? ? D MG 9999 D CYS 186  1_555 ? ? ? ? ? ? ?            2.230 ? 
metalc20 metalc ? ? W MG . MG ? ? ? 1_555 L  ASP 140 OD2 ? ? D MG 9999 D ASP 140  1_555 ? ? ? ? ? ? ?            2.222 ? 
metalc21 metalc ? ? W MG . MG ? ? ? 1_555 FA HOH .   O   ? ? D MG 9999 L HOH 55   1_555 ? ? ? ? ? ? ?            2.247 ? 
metalc22 metalc ? ? W MG . MG ? ? ? 1_555 X  ACY .   OXT ? ? D MG 9999 D ACY 5004 1_555 ? ? ? ? ? ? ?            2.329 ? 
metalc23 metalc ? ? W MG . MG ? ? ? 1_555 H  DC  1   OP2 ? ? D MG 9999 L DC  5    1_555 ? ? ? ? ? ? ?            2.160 ? 
metalc24 metalc ? ? M MG . MG ? ? ? 1_555 B  DC  1   OP3 ? ? I MG 2222 I DC  5    1_555 ? ? ? ? ? ? ?            3.063 ? 
metalc25 metalc ? ? M MG . MG ? ? ? 1_555 B  DC  1   OP2 ? ? I MG 2222 I DC  5    1_555 ? ? ? ? ? ? ?            2.295 ? 
metalc26 metalc ? ? M MG . MG ? ? ? 1_555 J  ASP 140 OD1 ? ? I MG 2222 B ASP 140  1_555 ? ? ? ? ? ? ?            2.048 ? 
metalc27 metalc ? ? M MG . MG ? ? ? 1_555 Z  HOH .   O   ? ? I MG 2222 I HOH 259  1_555 ? ? ? ? ? ? ?            2.205 ? 
metalc28 metalc ? ? M MG . MG ? ? ? 1_555 HA HOH .   O   ? ? I MG 2222 B HOH 3345 1_555 ? ? ? ? ? ? ?            2.146 ? 
metalc29 metalc ? ? M MG . MG ? ? ? 1_555 HA HOH .   O   ? ? I MG 2222 B HOH 3403 1_555 ? ? ? ? ? ? ?            2.271 ? 
metalc30 metalc ? ? M MG . MG ? ? ? 1_555 T  ACY .   O   ? ? I MG 2222 B ACY 3002 1_555 ? ? ? ? ? ? ?            2.148 ? 
metalc31 metalc ? ? N MG . MG ? ? ? 1_555 R  ACY .   OXT ? ? J MG 4444 A ACY 2001 1_555 ? ? ? ? ? ? ?            2.109 ? 
metalc32 metalc ? ? N MG . MG ? ? ? 1_555 GA HOH .   O   ? ? J MG 4444 A HOH 5562 1_555 ? ? ? ? ? ? ?            2.296 ? 
metalc33 metalc ? ? N MG . MG ? ? ? 1_555 AA HOH .   O   ? ? J MG 4444 F HOH 22   1_555 ? ? ? ? ? ? ?            2.195 ? 
metalc34 metalc ? ? N MG . MG ? ? ? 1_555 D  DC  1   OP3 ? ? J MG 4444 J DC  5    1_555 ? ? ? ? ? ? ?            2.907 ? 
metalc35 metalc ? ? N MG . MG ? ? ? 1_555 D  DC  1   OP2 ? ? J MG 4444 J DC  5    1_555 ? ? ? ? ? ? ?            2.289 ? 
metalc36 metalc ? ? N MG . MG ? ? ? 1_555 I  ASP 140 OD1 ? ? J MG 4444 A ASP 140  1_555 ? ? ? ? ? ? ?            2.151 ? 
metalc37 metalc ? ? N MG . MG ? ? ? 1_555 GA HOH .   O   ? ? J MG 4444 A HOH 5593 1_555 ? ? ? ? ? ? ?            2.322 ? 
metalc38 metalc ? ? O MG . MG ? ? ? 1_555 F  DC  1   OP3 ? ? K MG 6666 K DC  5    1_555 ? ? ? ? ? ? ?            2.939 ? 
metalc39 metalc ? ? O MG . MG ? ? ? 1_555 V  ACY .   OXT ? ? K MG 6666 C ACY 4003 1_555 ? ? ? ? ? ? ?            2.187 ? 
metalc40 metalc ? ? O MG . MG ? ? ? 1_555 F  DC  1   OP2 ? ? K MG 6666 K DC  5    1_555 ? ? ? ? ? ? ?            2.307 ? 
metalc41 metalc ? ? O MG . MG ? ? ? 1_555 IA HOH .   O   ? ? K MG 6666 C HOH 7780 1_555 ? ? ? ? ? ? ?            2.334 ? 
metalc42 metalc ? ? O MG . MG ? ? ? 1_555 DA HOH .   O   ? ? K MG 6666 K HOH 271  1_555 ? ? ? ? ? ? ?            2.188 ? 
metalc43 metalc ? ? O MG . MG ? ? ? 1_555 IA HOH .   O   ? ? K MG 6666 C HOH 7779 1_555 ? ? ? ? ? ? ?            2.242 ? 
metalc44 metalc ? ? O MG . MG ? ? ? 1_555 K  ASP 140 OD1 ? ? K MG 6666 C ASP 140  1_555 ? ? ? ? ? ? ?            2.096 ? 
metalc45 metalc ? ? P MG . MG ? ? ? 1_555 L  ASP 140 OD1 ? ? L MG 8888 D ASP 140  1_555 ? ? ? ? ? ? ?            2.147 ? 
metalc46 metalc ? ? P MG . MG ? ? ? 1_555 H  DC  1   OP3 ? ? L MG 8888 L DC  5    1_555 ? ? ? ? ? ? ?            3.052 ? 
metalc47 metalc ? ? P MG . MG ? ? ? 1_555 X  ACY .   O   ? ? L MG 8888 D ACY 5004 1_555 ? ? ? ? ? ? ?            2.153 ? 
metalc48 metalc ? ? P MG . MG ? ? ? 1_555 H  DC  1   OP2 ? ? L MG 8888 L DC  5    1_555 ? ? ? ? ? ? ?            2.253 ? 
metalc49 metalc ? ? P MG . MG ? ? ? 1_555 JA HOH .   O   ? ? L MG 8888 D HOH 1109 1_555 ? ? ? ? ? ? ?            2.206 ? 
metalc50 metalc ? ? P MG . MG ? ? ? 1_555 JA HOH .   O   ? ? L MG 8888 D HOH 1026 1_555 ? ? ? ? ? ? ?            2.372 ? 
metalc51 metalc ? ? P MG . MG ? ? ? 1_555 JA HOH .   O   ? ? L MG 8888 D HOH 1118 1_555 ? ? ? ? ? ? ?            2.204 ? 
metalc52 metalc ? ? W MG . MG ? ? ? 1_555 JA HOH .   O   ? ? D MG 9999 D HOH 1022 1_555 ? ? ? ? ? ? ?            2.236 ? 
hydrog1  hydrog ? ? A DG 2 N1 ? ? ? 1_555 D  DC  7   N3  ? ? E DG 2    J DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog2  hydrog ? ? A DG 2 N2 ? ? ? 1_555 D  DC  7   O2  ? ? E DG 2    J DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog3  hydrog ? ? A DG 2 O6 ? ? ? 1_555 D  DC  7   N4  ? ? E DG 2    J DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog4  hydrog ? ? A DC 3 N3 ? ? ? 1_555 D  DG  6   N1  ? ? E DC 3    J DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog5  hydrog ? ? A DC 3 N4 ? ? ? 1_555 D  DG  6   O6  ? ? E DC 3    J DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog6  hydrog ? ? A DC 3 O2 ? ? ? 1_555 D  DG  6   N2  ? ? E DC 3    J DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog7  hydrog ? ? A DG 4 N1 ? ? ? 1_555 D  DC  5   N3  ? ? E DG 4    J DC  9    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog8  hydrog ? ? A DG 4 N2 ? ? ? 1_555 D  DC  5   O2  ? ? E DG 4    J DC  9    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog9  hydrog ? ? A DG 4 O6 ? ? ? 1_555 D  DC  5   N4  ? ? E DG 4    J DC  9    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog10 hydrog ? ? B DC 1 N3 ? ? ? 1_555 D  DG  4   N1  ? ? I DC 5    J DG  8    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog11 hydrog ? ? B DC 1 N4 ? ? ? 1_555 D  DG  4   O6  ? ? I DC 5    J DG  8    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog12 hydrog ? ? B DC 1 O2 ? ? ? 1_555 D  DG  4   N2  ? ? I DC 5    J DG  8    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog13 hydrog ? ? B DC 2 N3 ? ? ? 1_555 D  DG  3   N1  ? ? I DC 6    J DG  7    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog14 hydrog ? ? B DC 2 N4 ? ? ? 1_555 D  DG  3   O6  ? ? I DC 6    J DG  7    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog15 hydrog ? ? B DC 2 O2 ? ? ? 1_555 D  DG  3   N2  ? ? I DC 6    J DG  7    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog16 hydrog ? ? B DG 3 N1 ? ? ? 1_555 D  DC  2   N3  ? ? I DG 7    J DC  6    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog17 hydrog ? ? B DG 3 N2 ? ? ? 1_555 D  DC  2   O2  ? ? I DG 7    J DC  6    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog18 hydrog ? ? B DG 3 O6 ? ? ? 1_555 D  DC  2   N4  ? ? I DG 7    J DC  6    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog19 hydrog ? ? B DG 4 N1 ? ? ? 1_555 D  DC  1   N3  ? ? I DG 8    J DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog20 hydrog ? ? B DG 4 N2 ? ? ? 1_555 D  DC  1   O2  ? ? I DG 8    J DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog21 hydrog ? ? B DG 4 O6 ? ? ? 1_555 D  DC  1   N4  ? ? I DG 8    J DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog22 hydrog ? ? B DC 5 N3 ? ? ? 1_555 C  DG  4   N1  ? ? I DC 9    F DG  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog23 hydrog ? ? B DC 5 N4 ? ? ? 1_555 C  DG  4   O6  ? ? I DC 9    F DG  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog24 hydrog ? ? B DC 5 O2 ? ? ? 1_555 C  DG  4   N2  ? ? I DC 9    F DG  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog25 hydrog ? ? B DG 6 N1 ? ? ? 1_555 C  DC  3   N3  ? ? I DG 10   F DC  3    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog26 hydrog ? ? B DG 6 N2 ? ? ? 1_555 C  DC  3   O2  ? ? I DG 10   F DC  3    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog27 hydrog ? ? B DG 6 O6 ? ? ? 1_555 C  DC  3   N4  ? ? I DG 10   F DC  3    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog28 hydrog ? ? B DC 7 N3 ? ? ? 1_555 C  DG  2   N1  ? ? I DC 11   F DG  2    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog29 hydrog ? ? B DC 7 N4 ? ? ? 1_555 C  DG  2   O6  ? ? I DC 11   F DG  2    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog30 hydrog ? ? B DC 7 O2 ? ? ? 1_555 C  DG  2   N2  ? ? I DC 11   F DG  2    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog31 hydrog ? ? E DG 2 N1 ? ? ? 1_555 H  DC  7   N3  ? ? G DG 2    L DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog32 hydrog ? ? E DG 2 N2 ? ? ? 1_555 H  DC  7   O2  ? ? G DG 2    L DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog33 hydrog ? ? E DG 2 O6 ? ? ? 1_555 H  DC  7   N4  ? ? G DG 2    L DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog34 hydrog ? ? E DC 3 N3 ? ? ? 1_555 H  DG  6   N1  ? ? G DC 3    L DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog35 hydrog ? ? E DC 3 N4 ? ? ? 1_555 H  DG  6   O6  ? ? G DC 3    L DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog36 hydrog ? ? E DC 3 O2 ? ? ? 1_555 H  DG  6   N2  ? ? G DC 3    L DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog37 hydrog ? ? E DG 4 N1 ? ? ? 1_555 H  DC  5   N3  ? ? G DG 4    L DC  9    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog38 hydrog ? ? E DG 4 N2 ? ? ? 1_555 H  DC  5   O2  ? ? G DG 4    L DC  9    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog39 hydrog ? ? E DG 4 O6 ? ? ? 1_555 H  DC  5   N4  ? ? G DG 4    L DC  9    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog40 hydrog ? ? F DC 1 N3 ? ? ? 1_555 H  DG  4   N1  ? ? K DC 5    L DG  8    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog41 hydrog ? ? F DC 1 N4 ? ? ? 1_555 H  DG  4   O6  ? ? K DC 5    L DG  8    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog42 hydrog ? ? F DC 1 O2 ? ? ? 1_555 H  DG  4   N2  ? ? K DC 5    L DG  8    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog43 hydrog ? ? F DC 2 N3 ? ? ? 1_555 H  DG  3   N1  ? ? K DC 6    L DG  7    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog44 hydrog ? ? F DC 2 N4 ? ? ? 1_555 H  DG  3   O6  ? ? K DC 6    L DG  7    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog45 hydrog ? ? F DC 2 O2 ? ? ? 1_555 H  DG  3   N2  ? ? K DC 6    L DG  7    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog46 hydrog ? ? F DG 3 N1 ? ? ? 1_555 H  DC  2   N3  ? ? K DG 7    L DC  6    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog47 hydrog ? ? F DG 3 N2 ? ? ? 1_555 H  DC  2   O2  ? ? K DG 7    L DC  6    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog48 hydrog ? ? F DG 3 O6 ? ? ? 1_555 H  DC  2   N4  ? ? K DG 7    L DC  6    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog49 hydrog ? ? F DG 4 N1 ? ? ? 1_555 H  DC  1   N3  ? ? K DG 8    L DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog50 hydrog ? ? F DG 4 N2 ? ? ? 1_555 H  DC  1   O2  ? ? K DG 8    L DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog51 hydrog ? ? F DG 4 O6 ? ? ? 1_555 H  DC  1   N4  ? ? K DG 8    L DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog52 hydrog ? ? F DC 5 N3 ? ? ? 1_555 G  DG  4   N1  ? ? K DC 9    H DG  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog53 hydrog ? ? F DC 5 N4 ? ? ? 1_555 G  DG  4   O6  ? ? K DC 9    H DG  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog54 hydrog ? ? F DC 5 O2 ? ? ? 1_555 G  DG  4   N2  ? ? K DC 9    H DG  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog55 hydrog ? ? F DG 6 N1 ? ? ? 1_555 G  DC  3   N3  ? ? K DG 10   H DC  3    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog56 hydrog ? ? F DG 6 N2 ? ? ? 1_555 G  DC  3   O2  ? ? K DG 10   H DC  3    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog57 hydrog ? ? F DG 6 O6 ? ? ? 1_555 G  DC  3   N4  ? ? K DG 10   H DC  3    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog58 hydrog ? ? F DC 7 N3 ? ? ? 1_555 G  DG  2   N1  ? ? K DC 11   H DG  2    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog59 hydrog ? ? F DC 7 N4 ? ? ? 1_555 G  DG  2   O6  ? ? K DC 11   H DG  2    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog60 hydrog ? ? F DC 7 O2 ? ? ? 1_555 G  DG  2   N2  ? ? K DC 11   H DG  2    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
metalc ? ? 
hydrog ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 6 ? 
B ? 6 ? 
C ? 6 ? 
D ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? parallel      
A 4 5 ? parallel      
A 5 6 ? parallel      
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? parallel      
B 4 5 ? parallel      
B 5 6 ? parallel      
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? parallel      
D 4 5 ? parallel      
D 5 6 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 TRP I 92  ? GLN I 96  ? TRP A 92  GLN A 96  
A 2 ILE I 141 ? ARG I 145 ? ILE A 141 ARG A 145 
A 3 LEU I 179 ? LYS I 187 ? LEU A 179 LYS A 187 
A 4 HIS I 215 ? THR I 220 ? HIS A 215 THR A 220 
A 5 CYS I 240 ? HIS I 243 ? CYS A 240 HIS A 243 
A 6 LEU I 274 ? ASP I 276 ? LEU A 274 ASP A 276 
B 1 TRP J 92  ? GLN J 96  ? TRP B 92  GLN B 96  
B 2 ILE J 141 ? ARG J 145 ? ILE B 141 ARG B 145 
B 3 LEU J 179 ? LYS J 187 ? LEU B 179 LYS B 187 
B 4 HIS J 215 ? THR J 220 ? HIS B 215 THR B 220 
B 5 CYS J 240 ? HIS J 243 ? CYS B 240 HIS B 243 
B 6 LEU J 274 ? ASP J 276 ? LEU B 274 ASP B 276 
C 1 TRP K 92  ? GLN K 96  ? TRP C 92  GLN C 96  
C 2 ILE K 141 ? ARG K 145 ? ILE C 141 ARG C 145 
C 3 LEU K 179 ? LYS K 187 ? LEU C 179 LYS C 187 
C 4 HIS K 215 ? THR K 220 ? HIS C 215 THR C 220 
C 5 CYS K 240 ? HIS K 243 ? CYS C 240 HIS C 243 
C 6 LEU K 274 ? ASP K 276 ? LEU C 274 ASP C 276 
D 1 TRP L 92  ? GLN L 96  ? TRP D 92  GLN D 96  
D 2 ILE L 141 ? ARG L 145 ? ILE D 141 ARG D 145 
D 3 LEU L 179 ? LYS L 187 ? LEU D 179 LYS D 187 
D 4 HIS L 215 ? THR L 220 ? HIS D 215 THR D 220 
D 5 CYS L 240 ? HIS L 243 ? CYS D 240 HIS D 243 
D 6 LEU L 274 ? ASP L 276 ? LEU D 274 ASP D 276 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N LYS I 95  ? N LYS A 95  O ILE I 142 ? O ILE A 142 
A 2 3 O ARG I 145 ? O ARG A 145 N LEU I 179 ? N LEU A 179 
A 3 4 O HIS I 181 ? O HIS A 181 N HIS I 215 ? N HIS A 215 
A 4 5 N VAL I 218 ? N VAL A 218 O CYS I 240 ? O CYS A 240 
A 5 6 N HIS I 243 ? N HIS A 243 O LYS I 275 ? O LYS A 275 
B 1 2 N LYS J 95  ? N LYS B 95  O ILE J 142 ? O ILE B 142 
B 2 3 O ARG J 145 ? O ARG B 145 N LEU J 179 ? N LEU B 179 
B 3 4 O HIS J 181 ? O HIS B 181 N HIS J 215 ? N HIS B 215 
B 4 5 N VAL J 218 ? N VAL B 218 O CYS J 240 ? O CYS B 240 
B 5 6 N HIS J 243 ? N HIS B 243 O LYS J 275 ? O LYS B 275 
C 1 2 O LYS K 95  ? O LYS C 95  N ILE K 142 ? N ILE C 142 
C 2 3 N ARG K 145 ? N ARG C 145 O LEU K 179 ? O LEU C 179 
C 3 4 O HIS K 181 ? O HIS C 181 N HIS K 215 ? N HIS C 215 
C 4 5 N VAL K 218 ? N VAL C 218 O CYS K 240 ? O CYS C 240 
C 5 6 N HIS K 243 ? N HIS C 243 O LYS K 275 ? O LYS C 275 
D 1 2 O LYS L 95  ? O LYS D 95  N ILE L 142 ? N ILE D 142 
D 2 3 N ARG L 145 ? N ARG D 145 O LEU L 179 ? O LEU D 179 
D 3 4 O HIS L 181 ? O HIS D 181 N HIS L 215 ? N HIS D 215 
D 4 5 N VAL L 218 ? N VAL D 218 O CYS L 240 ? O CYS D 240 
D 5 6 N HIS L 243 ? N HIS D 243 O LYS L 275 ? O LYS D 275 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MG I 2222'  
AC2 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MG J 4444'  
AC3 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MG K 6666'  
AC4 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MG L 8888'  
AC5 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MG A 5555'  
AC6 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE ACY A 2001' 
AC7 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MG B 3333'  
AC8 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE ACY B 3002' 
AC9 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MG C 7777'  
BC1 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE ACY C 4003' 
BC2 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MG D 9999'  
BC3 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE ACY D 5004' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 7  ASP J  140 ? ASP B 140  . ? 1_555 ? 
2   AC1 7  ACY T  .   ? ACY B 3002 . ? 1_555 ? 
3   AC1 7  MG  S  .   ? MG  B 3333 . ? 1_555 ? 
4   AC1 7  HOH HA .   ? HOH B 3345 . ? 1_555 ? 
5   AC1 7  HOH HA .   ? HOH B 3403 . ? 1_555 ? 
6   AC1 7  DC  B  1   ? DC  I 5    . ? 1_555 ? 
7   AC1 7  HOH Z  .   ? HOH I 259  . ? 1_555 ? 
8   AC2 7  ASP I  140 ? ASP A 140  . ? 1_555 ? 
9   AC2 7  ACY R  .   ? ACY A 2001 . ? 1_555 ? 
10  AC2 7  MG  Q  .   ? MG  A 5555 . ? 1_555 ? 
11  AC2 7  HOH GA .   ? HOH A 5562 . ? 1_555 ? 
12  AC2 7  HOH GA .   ? HOH A 5593 . ? 1_555 ? 
13  AC2 7  HOH AA .   ? HOH F 22   . ? 1_555 ? 
14  AC2 7  DC  D  1   ? DC  J 5    . ? 1_555 ? 
15  AC3 7  ASP K  140 ? ASP C 140  . ? 1_555 ? 
16  AC3 7  ACY V  .   ? ACY C 4003 . ? 1_555 ? 
17  AC3 7  MG  U  .   ? MG  C 7777 . ? 1_555 ? 
18  AC3 7  HOH IA .   ? HOH C 7779 . ? 1_555 ? 
19  AC3 7  HOH IA .   ? HOH C 7780 . ? 1_555 ? 
20  AC3 7  DC  F  1   ? DC  K 5    . ? 1_555 ? 
21  AC3 7  HOH DA .   ? HOH K 271  . ? 1_555 ? 
22  AC4 7  ASP L  140 ? ASP D 140  . ? 1_555 ? 
23  AC4 7  HOH JA .   ? HOH D 1026 . ? 1_555 ? 
24  AC4 7  HOH JA .   ? HOH D 1109 . ? 1_555 ? 
25  AC4 7  HOH JA .   ? HOH D 1118 . ? 1_555 ? 
26  AC4 7  ACY X  .   ? ACY D 5004 . ? 1_555 ? 
27  AC4 7  MG  W  .   ? MG  D 9999 . ? 1_555 ? 
28  AC4 7  DC  H  1   ? DC  L 5    . ? 1_555 ? 
29  AC5 7  ASP I  140 ? ASP A 140  . ? 1_555 ? 
30  AC5 7  CYS I  186 ? CYS A 186  . ? 1_555 ? 
31  AC5 7  ACY R  .   ? ACY A 2001 . ? 1_555 ? 
32  AC5 7  HOH GA .   ? HOH A 5564 . ? 1_555 ? 
33  AC5 7  DC  D  1   ? DC  J 5    . ? 1_555 ? 
34  AC5 7  HOH BA .   ? HOH J 221  . ? 1_555 ? 
35  AC5 7  MG  N  .   ? MG  J 4444 . ? 1_555 ? 
36  AC6 12 ASP I  140 ? ASP A 140  . ? 1_555 ? 
37  AC6 12 SER I  185 ? SER A 185  . ? 1_555 ? 
38  AC6 12 CYS I  186 ? CYS A 186  . ? 1_555 ? 
39  AC6 12 LYS I  187 ? LYS A 187  . ? 1_555 ? 
40  AC6 12 ASN I  197 ? ASN A 197  . ? 1_555 ? 
41  AC6 12 ALA I  198 ? ALA A 198  . ? 1_555 ? 
42  AC6 12 MG  Q  .   ? MG  A 5555 . ? 1_555 ? 
43  AC6 12 HOH GA .   ? HOH A 5562 . ? 1_555 ? 
44  AC6 12 HOH GA .   ? HOH A 5593 . ? 1_555 ? 
45  AC6 12 DC  D  1   ? DC  J 5    . ? 1_555 ? 
46  AC6 12 HOH BA .   ? HOH J 221  . ? 1_555 ? 
47  AC6 12 MG  N  .   ? MG  J 4444 . ? 1_555 ? 
48  AC7 7  ASP J  140 ? ASP B 140  . ? 1_555 ? 
49  AC7 7  CYS J  186 ? CYS B 186  . ? 1_555 ? 
50  AC7 7  ACY T  .   ? ACY B 3002 . ? 1_555 ? 
51  AC7 7  HOH HA .   ? HOH B 3390 . ? 1_555 ? 
52  AC7 7  DC  B  1   ? DC  I 5    . ? 1_555 ? 
53  AC7 7  HOH Z  .   ? HOH I 57   . ? 1_555 ? 
54  AC7 7  MG  M  .   ? MG  I 2222 . ? 1_555 ? 
55  AC8 13 ASP J  140 ? ASP B 140  . ? 1_555 ? 
56  AC8 13 SER J  185 ? SER B 185  . ? 1_555 ? 
57  AC8 13 CYS J  186 ? CYS B 186  . ? 1_555 ? 
58  AC8 13 LYS J  187 ? LYS B 187  . ? 1_555 ? 
59  AC8 13 ASN J  197 ? ASN B 197  . ? 1_555 ? 
60  AC8 13 ALA J  198 ? ALA B 198  . ? 1_555 ? 
61  AC8 13 MG  S  .   ? MG  B 3333 . ? 1_555 ? 
62  AC8 13 HOH HA .   ? HOH B 3384 . ? 1_555 ? 
63  AC8 13 HOH HA .   ? HOH B 3403 . ? 1_555 ? 
64  AC8 13 DC  B  1   ? DC  I 5    . ? 1_555 ? 
65  AC8 13 HOH Z  .   ? HOH I 57   . ? 1_555 ? 
66  AC8 13 HOH Z  .   ? HOH I 259  . ? 1_555 ? 
67  AC8 13 MG  M  .   ? MG  I 2222 . ? 1_555 ? 
68  AC9 7  ASP K  140 ? ASP C 140  . ? 1_555 ? 
69  AC9 7  CYS K  186 ? CYS C 186  . ? 1_555 ? 
70  AC9 7  ACY V  .   ? ACY C 4003 . ? 1_555 ? 
71  AC9 7  HOH IA .   ? HOH C 7781 . ? 1_555 ? 
72  AC9 7  DC  F  1   ? DC  K 5    . ? 1_555 ? 
73  AC9 7  HOH DA .   ? HOH K 328  . ? 1_555 ? 
74  AC9 7  MG  O  .   ? MG  K 6666 . ? 1_555 ? 
75  BC1 14 ASP K  140 ? ASP C 140  . ? 1_555 ? 
76  BC1 14 SER K  185 ? SER C 185  . ? 1_555 ? 
77  BC1 14 CYS K  186 ? CYS C 186  . ? 1_555 ? 
78  BC1 14 LYS K  187 ? LYS C 187  . ? 1_555 ? 
79  BC1 14 ASN K  197 ? ASN C 197  . ? 1_555 ? 
80  BC1 14 ALA K  198 ? ALA C 198  . ? 1_555 ? 
81  BC1 14 GLU K  201 ? GLU C 201  . ? 1_555 ? 
82  BC1 14 MG  U  .   ? MG  C 7777 . ? 1_555 ? 
83  BC1 14 HOH IA .   ? HOH C 7780 . ? 1_555 ? 
84  BC1 14 HOH IA .   ? HOH C 7829 . ? 1_555 ? 
85  BC1 14 DC  F  1   ? DC  K 5    . ? 1_555 ? 
86  BC1 14 HOH DA .   ? HOH K 271  . ? 1_555 ? 
87  BC1 14 HOH DA .   ? HOH K 328  . ? 1_555 ? 
88  BC1 14 MG  O  .   ? MG  K 6666 . ? 1_555 ? 
89  BC2 7  ASP L  140 ? ASP D 140  . ? 1_555 ? 
90  BC2 7  CYS L  186 ? CYS D 186  . ? 1_555 ? 
91  BC2 7  HOH JA .   ? HOH D 1022 . ? 1_555 ? 
92  BC2 7  ACY X  .   ? ACY D 5004 . ? 1_555 ? 
93  BC2 7  DC  H  1   ? DC  L 5    . ? 1_555 ? 
94  BC2 7  HOH FA .   ? HOH L 55   . ? 1_555 ? 
95  BC2 7  MG  P  .   ? MG  L 8888 . ? 1_555 ? 
96  BC3 13 ASP L  140 ? ASP D 140  . ? 1_555 ? 
97  BC3 13 SER L  185 ? SER D 185  . ? 1_555 ? 
98  BC3 13 CYS L  186 ? CYS D 186  . ? 1_555 ? 
99  BC3 13 LYS L  187 ? LYS D 187  . ? 1_555 ? 
100 BC3 13 ASN L  197 ? ASN D 197  . ? 1_555 ? 
101 BC3 13 ALA L  198 ? ALA D 198  . ? 1_555 ? 
102 BC3 13 HOH JA .   ? HOH D 1020 . ? 1_555 ? 
103 BC3 13 HOH JA .   ? HOH D 1026 . ? 1_555 ? 
104 BC3 13 HOH JA .   ? HOH D 1109 . ? 1_555 ? 
105 BC3 13 MG  W  .   ? MG  D 9999 . ? 1_555 ? 
106 BC3 13 DC  H  1   ? DC  L 5    . ? 1_555 ? 
107 BC3 13 HOH FA .   ? HOH L 55   . ? 1_555 ? 
108 BC3 13 MG  P  .   ? MG  L 8888 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1FIU 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1FIU 
_atom_sites.fract_transf_matrix[1][1]   0.011062 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010973 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006688 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     O  "O5'" . DT  A  1 1   ? 31.558  74.634  148.028 1.00 40.38 ? 1    DT  E "O5'" 1 
ATOM   2     C  "C5'" . DT  A  1 1   ? 31.940  74.996  149.363 1.00 39.14 ? 1    DT  E "C5'" 1 
ATOM   3     C  "C4'" . DT  A  1 1   ? 33.215  74.324  149.818 1.00 38.72 ? 1    DT  E "C4'" 1 
ATOM   4     O  "O4'" . DT  A  1 1   ? 33.031  72.884  149.840 1.00 35.09 ? 1    DT  E "O4'" 1 
ATOM   5     C  "C3'" . DT  A  1 1   ? 34.432  74.572  148.921 1.00 37.33 ? 1    DT  E "C3'" 1 
ATOM   6     O  "O3'" . DT  A  1 1   ? 35.605  74.640  149.745 1.00 40.95 ? 1    DT  E "O3'" 1 
ATOM   7     C  "C2'" . DT  A  1 1   ? 34.470  73.329  148.048 1.00 37.79 ? 1    DT  E "C2'" 1 
ATOM   8     C  "C1'" . DT  A  1 1   ? 34.024  72.263  149.029 1.00 40.06 ? 1    DT  E "C1'" 1 
ATOM   9     N  N1    . DT  A  1 1   ? 33.437  71.043  148.427 1.00 42.04 ? 1    DT  E N1    1 
ATOM   10    C  C2    . DT  A  1 1   ? 34.280  69.978  148.204 1.00 45.24 ? 1    DT  E C2    1 
ATOM   11    O  O2    . DT  A  1 1   ? 35.481  70.021  148.442 1.00 45.96 ? 1    DT  E O2    1 
ATOM   12    N  N3    . DT  A  1 1   ? 33.664  68.856  147.688 1.00 43.12 ? 1    DT  E N3    1 
ATOM   13    C  C4    . DT  A  1 1   ? 32.326  68.708  147.375 1.00 42.59 ? 1    DT  E C4    1 
ATOM   14    O  O4    . DT  A  1 1   ? 31.905  67.635  146.946 1.00 40.03 ? 1    DT  E O4    1 
ATOM   15    C  C5    . DT  A  1 1   ? 31.509  69.874  147.601 1.00 43.57 ? 1    DT  E C5    1 
ATOM   16    C  C7    . DT  A  1 1   ? 30.055  69.810  147.251 1.00 42.24 ? 1    DT  E C7    1 
ATOM   17    C  C6    . DT  A  1 1   ? 32.094  70.969  148.112 1.00 41.24 ? 1    DT  E C6    1 
ATOM   18    P  P     . DG  A  1 2   ? 36.989  75.206  149.137 1.00 41.65 ? 2    DG  E P     1 
ATOM   19    O  OP1   . DG  A  1 2   ? 37.887  75.531  150.275 1.00 37.75 ? 2    DG  E OP1   1 
ATOM   20    O  OP2   . DG  A  1 2   ? 36.688  76.249  148.119 1.00 44.94 ? 2    DG  E OP2   1 
ATOM   21    O  "O5'" . DG  A  1 2   ? 37.618  73.958  148.375 1.00 39.26 ? 2    DG  E "O5'" 1 
ATOM   22    C  "C5'" . DG  A  1 2   ? 38.092  72.828  149.105 1.00 39.56 ? 2    DG  E "C5'" 1 
ATOM   23    C  "C4'" . DG  A  1 2   ? 38.980  71.970  148.237 1.00 38.71 ? 2    DG  E "C4'" 1 
ATOM   24    O  "O4'" . DG  A  1 2   ? 38.225  71.372  147.158 1.00 40.34 ? 2    DG  E "O4'" 1 
ATOM   25    C  "C3'" . DG  A  1 2   ? 40.152  72.672  147.565 1.00 36.88 ? 2    DG  E "C3'" 1 
ATOM   26    O  "O3'" . DG  A  1 2   ? 41.199  71.704  147.497 1.00 34.69 ? 2    DG  E "O3'" 1 
ATOM   27    C  "C2'" . DG  A  1 2   ? 39.601  73.056  146.197 1.00 35.41 ? 2    DG  E "C2'" 1 
ATOM   28    C  "C1'" . DG  A  1 2   ? 38.555  71.976  145.902 1.00 36.46 ? 2    DG  E "C1'" 1 
ATOM   29    N  N9    . DG  A  1 2   ? 37.291  72.465  145.360 1.00 33.56 ? 2    DG  E N9    1 
ATOM   30    C  C8    . DG  A  1 2   ? 36.868  73.766  145.243 1.00 31.82 ? 2    DG  E C8    1 
ATOM   31    N  N7    . DG  A  1 2   ? 35.609  73.863  144.898 1.00 26.12 ? 2    DG  E N7    1 
ATOM   32    C  C5    . DG  A  1 2   ? 35.191  72.548  144.739 1.00 27.46 ? 2    DG  E C5    1 
ATOM   33    C  C6    . DG  A  1 2   ? 33.913  72.017  144.420 1.00 33.90 ? 2    DG  E C6    1 
ATOM   34    O  O6    . DG  A  1 2   ? 32.839  72.622  144.249 1.00 36.76 ? 2    DG  E O6    1 
ATOM   35    N  N1    . DG  A  1 2   ? 33.944  70.629  144.336 1.00 33.75 ? 2    DG  E N1    1 
ATOM   36    C  C2    . DG  A  1 2   ? 35.054  69.847  144.563 1.00 32.55 ? 2    DG  E C2    1 
ATOM   37    N  N2    . DG  A  1 2   ? 34.893  68.519  144.431 1.00 33.85 ? 2    DG  E N2    1 
ATOM   38    N  N3    . DG  A  1 2   ? 36.239  70.331  144.897 1.00 33.77 ? 2    DG  E N3    1 
ATOM   39    C  C4    . DG  A  1 2   ? 36.234  71.676  144.967 1.00 31.42 ? 2    DG  E C4    1 
ATOM   40    P  P     . DC  A  1 3   ? 42.589  72.054  146.777 1.00 38.76 ? 3    DC  E P     1 
ATOM   41    O  OP1   . DC  A  1 3   ? 43.640  71.333  147.546 1.00 39.07 ? 3    DC  E OP1   1 
ATOM   42    O  OP2   . DC  A  1 3   ? 42.726  73.518  146.535 1.00 39.80 ? 3    DC  E OP2   1 
ATOM   43    O  "O5'" . DC  A  1 3   ? 42.426  71.355  145.352 1.00 33.32 ? 3    DC  E "O5'" 1 
ATOM   44    C  "C5'" . DC  A  1 3   ? 41.896  70.040  145.252 1.00 29.53 ? 3    DC  E "C5'" 1 
ATOM   45    C  "C4'" . DC  A  1 3   ? 41.530  69.729  143.821 1.00 21.75 ? 3    DC  E "C4'" 1 
ATOM   46    O  "O4'" . DC  A  1 3   ? 40.336  70.442  143.429 1.00 24.78 ? 3    DC  E "O4'" 1 
ATOM   47    C  "C3'" . DC  A  1 3   ? 42.608  70.134  142.811 1.00 25.12 ? 3    DC  E "C3'" 1 
ATOM   48    O  "O3'" . DC  A  1 3   ? 42.647  69.146  141.781 1.00 23.92 ? 3    DC  E "O3'" 1 
ATOM   49    C  "C2'" . DC  A  1 3   ? 42.050  71.419  142.218 1.00 22.97 ? 3    DC  E "C2'" 1 
ATOM   50    C  "C1'" . DC  A  1 3   ? 40.578  71.080  142.178 1.00 20.98 ? 3    DC  E "C1'" 1 
ATOM   51    N  N1    . DC  A  1 3   ? 39.655  72.218  142.071 1.00 22.53 ? 3    DC  E N1    1 
ATOM   52    C  C2    . DC  A  1 3   ? 38.337  71.956  141.726 1.00 21.43 ? 3    DC  E C2    1 
ATOM   53    O  O2    . DC  A  1 3   ? 38.000  70.788  141.502 1.00 22.75 ? 3    DC  E O2    1 
ATOM   54    N  N3    . DC  A  1 3   ? 37.448  72.985  141.655 1.00 28.18 ? 3    DC  E N3    1 
ATOM   55    C  C4    . DC  A  1 3   ? 37.850  74.226  141.933 1.00 25.67 ? 3    DC  E C4    1 
ATOM   56    N  N4    . DC  A  1 3   ? 36.936  75.212  141.893 1.00 26.27 ? 3    DC  E N4    1 
ATOM   57    C  C5    . DC  A  1 3   ? 39.204  74.519  142.273 1.00 28.85 ? 3    DC  E C5    1 
ATOM   58    C  C6    . DC  A  1 3   ? 40.066  73.494  142.321 1.00 23.97 ? 3    DC  E C6    1 
ATOM   59    P  P     . DG  A  1 4   ? 43.713  67.944  141.870 1.00 25.28 ? 4    DG  E P     1 
ATOM   60    O  OP1   . DG  A  1 4   ? 43.706  67.359  143.238 1.00 25.76 ? 4    DG  E OP1   1 
ATOM   61    O  OP2   . DG  A  1 4   ? 45.004  68.429  141.286 1.00 26.93 ? 4    DG  E OP2   1 
ATOM   62    O  "O5'" . DG  A  1 4   ? 43.093  66.852  140.900 1.00 22.16 ? 4    DG  E "O5'" 1 
ATOM   63    C  "C5'" . DG  A  1 4   ? 41.952  66.086  141.297 1.00 21.13 ? 4    DG  E "C5'" 1 
ATOM   64    C  "C4'" . DG  A  1 4   ? 40.977  65.960  140.146 1.00 20.79 ? 4    DG  E "C4'" 1 
ATOM   65    O  "O4'" . DG  A  1 4   ? 40.412  67.255  139.833 1.00 22.81 ? 4    DG  E "O4'" 1 
ATOM   66    C  "C3'" . DG  A  1 4   ? 41.573  65.441  138.833 1.00 20.03 ? 4    DG  E "C3'" 1 
ATOM   67    O  "O3'" . DG  A  1 4   ? 40.556  64.704  138.155 1.00 20.66 ? 4    DG  E "O3'" 1 
ATOM   68    C  "C2'" . DG  A  1 4   ? 41.832  66.719  138.042 1.00 20.29 ? 4    DG  E "C2'" 1 
ATOM   69    C  "C1'" . DG  A  1 4   ? 40.650  67.574  138.461 1.00 22.62 ? 4    DG  E "C1'" 1 
ATOM   70    N  N9    . DG  A  1 4   ? 40.863  69.014  138.404 1.00 17.95 ? 4    DG  E N9    1 
ATOM   71    C  C8    . DG  A  1 4   ? 42.048  69.700  138.517 1.00 19.59 ? 4    DG  E C8    1 
ATOM   72    N  N7    . DG  A  1 4   ? 41.876  70.999  138.558 1.00 18.66 ? 4    DG  E N7    1 
ATOM   73    C  C5    . DG  A  1 4   ? 40.504  71.172  138.436 1.00 19.11 ? 4    DG  E C5    1 
ATOM   74    C  C6    . DG  A  1 4   ? 39.724  72.354  138.461 1.00 17.67 ? 4    DG  E C6    1 
ATOM   75    O  O6    . DG  A  1 4   ? 40.101  73.512  138.647 1.00 19.94 ? 4    DG  E O6    1 
ATOM   76    N  N1    . DG  A  1 4   ? 38.368  72.078  138.279 1.00 18.88 ? 4    DG  E N1    1 
ATOM   77    C  C2    . DG  A  1 4   ? 37.829  70.823  138.128 1.00 17.78 ? 4    DG  E C2    1 
ATOM   78    N  N2    . DG  A  1 4   ? 36.505  70.760  137.919 1.00 16.65 ? 4    DG  E N2    1 
ATOM   79    N  N3    . DG  A  1 4   ? 38.543  69.708  138.163 1.00 17.68 ? 4    DG  E N3    1 
ATOM   80    C  C4    . DG  A  1 4   ? 39.869  69.962  138.306 1.00 18.80 ? 4    DG  E C4    1 
ATOM   81    O  OP3   . DC  B  2 1   ? 41.620  63.929  136.025 1.00 22.87 ? 5    DC  I OP3   1 
ATOM   82    P  P     . DC  B  2 1   ? 40.891  63.567  134.748 1.00 18.54 ? 5    DC  I P     1 
ATOM   83    O  OP1   . DC  B  2 1   ? 41.611  63.986  133.477 1.00 18.11 ? 5    DC  I OP1   1 
ATOM   84    O  OP2   . DC  B  2 1   ? 40.427  62.146  134.730 1.00 20.64 ? 5    DC  I OP2   1 
ATOM   85    O  "O5'" . DC  B  2 1   ? 39.542  64.475  134.783 1.00 18.58 ? 5    DC  I "O5'" 1 
ATOM   86    C  "C5'" . DC  B  2 1   ? 38.353  63.959  135.374 1.00 19.06 ? 5    DC  I "C5'" 1 
ATOM   87    C  "C4'" . DC  B  2 1   ? 37.172  64.791  134.952 1.00 18.88 ? 5    DC  I "C4'" 1 
ATOM   88    O  "O4'" . DC  B  2 1   ? 37.265  66.031  135.703 1.00 18.05 ? 5    DC  I "O4'" 1 
ATOM   89    C  "C3'" . DC  B  2 1   ? 37.191  65.207  133.481 1.00 16.71 ? 5    DC  I "C3'" 1 
ATOM   90    O  "O3'" . DC  B  2 1   ? 36.382  64.367  132.687 1.00 16.74 ? 5    DC  I "O3'" 1 
ATOM   91    C  "C2'" . DC  B  2 1   ? 36.613  66.616  133.488 1.00 25.74 ? 5    DC  I "C2'" 1 
ATOM   92    C  "C1'" . DC  B  2 1   ? 36.807  67.126  134.902 1.00 19.53 ? 5    DC  I "C1'" 1 
ATOM   93    N  N1    . DC  B  2 1   ? 37.874  68.140  134.880 1.00 17.69 ? 5    DC  I N1    1 
ATOM   94    C  C2    . DC  B  2 1   ? 37.519  69.496  134.708 1.00 18.15 ? 5    DC  I C2    1 
ATOM   95    O  O2    . DC  B  2 1   ? 36.327  69.783  134.551 1.00 17.99 ? 5    DC  I O2    1 
ATOM   96    N  N3    . DC  B  2 1   ? 38.485  70.440  134.709 1.00 17.86 ? 5    DC  I N3    1 
ATOM   97    C  C4    . DC  B  2 1   ? 39.766  70.089  134.869 1.00 17.50 ? 5    DC  I C4    1 
ATOM   98    N  N4    . DC  B  2 1   ? 40.678  71.074  134.912 1.00 19.46 ? 5    DC  I N4    1 
ATOM   99    C  C5    . DC  B  2 1   ? 40.167  68.724  135.009 1.00 17.48 ? 5    DC  I C5    1 
ATOM   100   C  C6    . DC  B  2 1   ? 39.196  67.783  135.016 1.00 17.39 ? 5    DC  I C6    1 
ATOM   101   P  P     . DC  B  2 2   ? 36.710  64.189  131.114 1.00 17.35 ? 6    DC  I P     1 
ATOM   102   O  OP1   . DC  B  2 2   ? 35.946  63.025  130.656 1.00 20.18 ? 6    DC  I OP1   1 
ATOM   103   O  OP2   . DC  B  2 2   ? 38.168  64.247  130.846 1.00 17.18 ? 6    DC  I OP2   1 
ATOM   104   O  "O5'" . DC  B  2 2   ? 36.075  65.500  130.468 1.00 18.80 ? 6    DC  I "O5'" 1 
ATOM   105   C  "C5'" . DC  B  2 2   ? 34.715  65.805  130.728 1.00 18.55 ? 6    DC  I "C5'" 1 
ATOM   106   C  "C4'" . DC  B  2 2   ? 34.328  67.114  130.087 1.00 16.63 ? 6    DC  I "C4'" 1 
ATOM   107   O  "O4'" . DC  B  2 2   ? 34.995  68.215  130.742 1.00 17.03 ? 6    DC  I "O4'" 1 
ATOM   108   C  "C3'" . DC  B  2 2   ? 34.556  67.277  128.585 1.00 19.68 ? 6    DC  I "C3'" 1 
ATOM   109   O  "O3'" . DC  B  2 2   ? 33.292  67.723  128.042 1.00 22.17 ? 6    DC  I "O3'" 1 
ATOM   110   C  "C2'" . DC  B  2 2   ? 35.712  68.264  128.494 1.00 17.91 ? 6    DC  I "C2'" 1 
ATOM   111   C  "C1'" . DC  B  2 2   ? 35.620  69.066  129.792 1.00 18.39 ? 6    DC  I "C1'" 1 
ATOM   112   N  N1    . DC  B  2 2   ? 36.919  69.476  130.353 1.00 18.83 ? 6    DC  I N1    1 
ATOM   113   C  C2    . DC  B  2 2   ? 37.242  70.836  130.404 1.00 18.81 ? 6    DC  I C2    1 
ATOM   114   O  O2    . DC  B  2 2   ? 36.391  71.668  130.021 1.00 19.02 ? 6    DC  I O2    1 
ATOM   115   N  N3    . DC  B  2 2   ? 38.457  71.219  130.883 1.00 17.74 ? 6    DC  I N3    1 
ATOM   116   C  C4    . DC  B  2 2   ? 39.325  70.289  131.313 1.00 16.06 ? 6    DC  I C4    1 
ATOM   117   N  N4    . DC  B  2 2   ? 40.526  70.694  131.730 1.00 16.66 ? 6    DC  I N4    1 
ATOM   118   C  C5    . DC  B  2 2   ? 39.000  68.899  131.313 1.00 16.78 ? 6    DC  I C5    1 
ATOM   119   C  C6    . DC  B  2 2   ? 37.808  68.538  130.821 1.00 18.51 ? 6    DC  I C6    1 
ATOM   120   P  P     . DG  B  2 3   ? 33.203  68.685  126.740 1.00 20.92 ? 7    DG  I P     1 
ATOM   121   O  OP1   . DG  B  2 3   ? 31.745  68.654  126.426 1.00 25.92 ? 7    DG  I OP1   1 
ATOM   122   O  OP2   . DG  B  2 3   ? 34.179  68.382  125.663 1.00 24.74 ? 7    DG  I OP2   1 
ATOM   123   O  "O5'" . DG  B  2 3   ? 33.536  70.131  127.298 1.00 20.40 ? 7    DG  I "O5'" 1 
ATOM   124   C  "C5'" . DG  B  2 3   ? 32.597  70.861  128.067 1.00 21.03 ? 7    DG  I "C5'" 1 
ATOM   125   C  "C4'" . DG  B  2 3   ? 32.536  72.275  127.548 1.00 18.89 ? 7    DG  I "C4'" 1 
ATOM   126   O  "O4'" . DG  B  2 3   ? 33.839  72.900  127.701 1.00 20.37 ? 7    DG  I "O4'" 1 
ATOM   127   C  "C3'" . DG  B  2 3   ? 32.210  72.347  126.063 1.00 21.59 ? 7    DG  I "C3'" 1 
ATOM   128   O  "O3'" . DG  B  2 3   ? 31.310  73.450  125.902 1.00 24.75 ? 7    DG  I "O3'" 1 
ATOM   129   C  "C2'" . DG  B  2 3   ? 33.568  72.508  125.385 1.00 20.98 ? 7    DG  I "C2'" 1 
ATOM   130   C  "C1'" . DG  B  2 3   ? 34.467  73.135  126.446 1.00 20.14 ? 7    DG  I "C1'" 1 
ATOM   131   N  N9    . DG  B  2 3   ? 35.820  72.564  126.506 1.00 19.12 ? 7    DG  I N9    1 
ATOM   132   C  C8    . DG  B  2 3   ? 36.200  71.275  126.195 1.00 18.59 ? 7    DG  I C8    1 
ATOM   133   N  N7    . DG  B  2 3   ? 37.482  71.053  126.395 1.00 17.51 ? 7    DG  I N7    1 
ATOM   134   C  C5    . DG  B  2 3   ? 37.981  72.272  126.837 1.00 18.20 ? 7    DG  I C5    1 
ATOM   135   C  C6    . DG  B  2 3   ? 39.300  72.649  127.206 1.00 17.93 ? 7    DG  I C6    1 
ATOM   136   O  O6    . DG  B  2 3   ? 40.333  71.954  127.226 1.00 18.87 ? 7    DG  I O6    1 
ATOM   137   N  N1    . DG  B  2 3   ? 39.361  73.983  127.590 1.00 18.73 ? 7    DG  I N1    1 
ATOM   138   C  C2    . DG  B  2 3   ? 38.287  74.848  127.621 1.00 18.84 ? 7    DG  I C2    1 
ATOM   139   N  N2    . DG  B  2 3   ? 38.541  76.101  128.034 1.00 16.84 ? 7    DG  I N2    1 
ATOM   140   N  N3    . DG  B  2 3   ? 37.054  74.507  127.276 1.00 17.25 ? 7    DG  I N3    1 
ATOM   141   C  C4    . DG  B  2 3   ? 36.971  73.217  126.904 1.00 17.97 ? 7    DG  I C4    1 
ATOM   142   P  P     . DG  B  2 4   ? 30.968  74.022  124.446 1.00 23.89 ? 8    DG  I P     1 
ATOM   143   O  OP1   . DG  B  2 4   ? 29.581  74.561  124.594 1.00 30.36 ? 8    DG  I OP1   1 
ATOM   144   O  OP2   . DG  B  2 4   ? 31.268  73.048  123.370 1.00 28.91 ? 8    DG  I OP2   1 
ATOM   145   O  "O5'" . DG  B  2 4   ? 31.972  75.248  124.313 1.00 20.15 ? 8    DG  I "O5'" 1 
ATOM   146   C  "C5'" . DG  B  2 4   ? 32.040  76.214  125.358 1.00 20.03 ? 8    DG  I "C5'" 1 
ATOM   147   C  "C4'" . DG  B  2 4   ? 33.103  77.243  125.062 1.00 20.97 ? 8    DG  I "C4'" 1 
ATOM   148   O  "O4'" . DG  B  2 4   ? 34.425  76.660  125.192 1.00 23.05 ? 8    DG  I "O4'" 1 
ATOM   149   C  "C3'" . DG  B  2 4   ? 33.033  77.850  123.661 1.00 20.04 ? 8    DG  I "C3'" 1 
ATOM   150   O  "O3'" . DG  B  2 4   ? 33.198  79.259  123.817 1.00 23.14 ? 8    DG  I "O3'" 1 
ATOM   151   C  "C2'" . DG  B  2 4   ? 34.207  77.195  122.933 1.00 20.45 ? 8    DG  I "C2'" 1 
ATOM   152   C  "C1'" . DG  B  2 4   ? 35.209  76.991  124.058 1.00 19.93 ? 8    DG  I "C1'" 1 
ATOM   153   N  N9    . DG  B  2 4   ? 36.165  75.906  123.853 1.00 17.23 ? 8    DG  I N9    1 
ATOM   154   C  C8    . DG  B  2 4   ? 35.889  74.636  123.403 1.00 19.55 ? 8    DG  I C8    1 
ATOM   155   N  N7    . DG  B  2 4   ? 36.956  73.877  123.314 1.00 19.20 ? 8    DG  I N7    1 
ATOM   156   C  C5    . DG  B  2 4   ? 37.999  74.694  123.731 1.00 16.42 ? 8    DG  I C5    1 
ATOM   157   C  C6    . DG  B  2 4   ? 39.408  74.418  123.831 1.00 17.44 ? 8    DG  I C6    1 
ATOM   158   O  O6    . DG  B  2 4   ? 40.003  73.369  123.574 1.00 18.16 ? 8    DG  I O6    1 
ATOM   159   N  N1    . DG  B  2 4   ? 40.116  75.522  124.280 1.00 17.52 ? 8    DG  I N1    1 
ATOM   160   C  C2    . DG  B  2 4   ? 39.552  76.737  124.609 1.00 16.34 ? 8    DG  I C2    1 
ATOM   161   N  N2    . DG  B  2 4   ? 40.406  77.663  125.042 1.00 19.16 ? 8    DG  I N2    1 
ATOM   162   N  N3    . DG  B  2 4   ? 38.236  77.007  124.520 1.00 15.38 ? 8    DG  I N3    1 
ATOM   163   C  C4    . DG  B  2 4   ? 37.532  75.949  124.073 1.00 16.53 ? 8    DG  I C4    1 
ATOM   164   P  P     . DC  B  2 5   ? 32.965  80.250  122.568 1.00 26.02 ? 9    DC  I P     1 
ATOM   165   O  OP1   . DC  B  2 5   ? 32.604  81.566  123.160 1.00 31.32 ? 9    DC  I OP1   1 
ATOM   166   O  OP2   . DC  B  2 5   ? 32.090  79.604  121.571 1.00 25.57 ? 9    DC  I OP2   1 
ATOM   167   O  "O5'" . DC  B  2 5   ? 34.413  80.368  121.926 1.00 22.35 ? 9    DC  I "O5'" 1 
ATOM   168   C  "C5'" . DC  B  2 5   ? 35.458  81.016  122.626 1.00 21.23 ? 9    DC  I "C5'" 1 
ATOM   169   C  "C4'" . DC  B  2 5   ? 36.718  80.965  121.800 1.00 20.04 ? 9    DC  I "C4'" 1 
ATOM   170   O  "O4'" . DC  B  2 5   ? 37.237  79.620  121.819 1.00 20.25 ? 9    DC  I "O4'" 1 
ATOM   171   C  "C3'" . DC  B  2 5   ? 36.514  81.313  120.321 1.00 21.50 ? 9    DC  I "C3'" 1 
ATOM   172   O  "O3'" . DC  B  2 5   ? 37.531  82.208  119.916 1.00 22.73 ? 9    DC  I "O3'" 1 
ATOM   173   C  "C2'" . DC  B  2 5   ? 36.732  79.992  119.597 1.00 20.80 ? 9    DC  I "C2'" 1 
ATOM   174   C  "C1'" . DC  B  2 5   ? 37.718  79.307  120.532 1.00 19.15 ? 9    DC  I "C1'" 1 
ATOM   175   N  N1    . DC  B  2 5   ? 37.830  77.845  120.449 1.00 20.15 ? 9    DC  I N1    1 
ATOM   176   C  C2    . DC  B  2 5   ? 39.100  77.243  120.599 1.00 18.86 ? 9    DC  I C2    1 
ATOM   177   O  O2    . DC  B  2 5   ? 40.089  77.959  120.841 1.00 19.96 ? 9    DC  I O2    1 
ATOM   178   N  N3    . DC  B  2 5   ? 39.197  75.886  120.495 1.00 17.92 ? 9    DC  I N3    1 
ATOM   179   C  C4    . DC  B  2 5   ? 38.096  75.153  120.281 1.00 19.35 ? 9    DC  I C4    1 
ATOM   180   N  N4    . DC  B  2 5   ? 38.233  73.828  120.175 1.00 19.72 ? 9    DC  I N4    1 
ATOM   181   C  C5    . DC  B  2 5   ? 36.802  75.744  120.159 1.00 20.33 ? 9    DC  I C5    1 
ATOM   182   C  C6    . DC  B  2 5   ? 36.717  77.072  120.240 1.00 21.24 ? 9    DC  I C6    1 
ATOM   183   P  P     . DG  B  2 6   ? 37.229  83.780  119.859 1.00 24.71 ? 10   DG  I P     1 
ATOM   184   O  OP1   . DG  B  2 6   ? 36.507  84.165  121.082 1.00 24.73 ? 10   DG  I OP1   1 
ATOM   185   O  OP2   . DG  B  2 6   ? 36.619  84.043  118.539 1.00 27.86 ? 10   DG  I OP2   1 
ATOM   186   O  "O5'" . DG  B  2 6   ? 38.701  84.395  119.885 1.00 24.27 ? 10   DG  I "O5'" 1 
ATOM   187   C  "C5'" . DG  B  2 6   ? 39.449  84.419  121.106 1.00 22.64 ? 10   DG  I "C5'" 1 
ATOM   188   C  "C4'" . DG  B  2 6   ? 40.918  84.194  120.833 1.00 23.65 ? 10   DG  I "C4'" 1 
ATOM   189   O  "O4'" . DG  B  2 6   ? 41.140  82.876  120.286 1.00 24.20 ? 10   DG  I "O4'" 1 
ATOM   190   C  "C3'" . DG  B  2 6   ? 41.555  85.148  119.832 1.00 25.23 ? 10   DG  I "C3'" 1 
ATOM   191   O  "O3'" . DG  B  2 6   ? 42.937  85.205  120.179 1.00 29.26 ? 10   DG  I "O3'" 1 
ATOM   192   C  "C2'" . DG  B  2 6   ? 41.338  84.430  118.512 1.00 26.11 ? 10   DG  I "C2'" 1 
ATOM   193   C  "C1'" . DG  B  2 6   ? 41.488  82.961  118.902 1.00 29.00 ? 10   DG  I "C1'" 1 
ATOM   194   N  N9    . DG  B  2 6   ? 40.615  82.022  118.201 1.00 27.93 ? 10   DG  I N9    1 
ATOM   195   C  C8    . DG  B  2 6   ? 39.364  82.259  117.685 1.00 27.50 ? 10   DG  I C8    1 
ATOM   196   N  N7    . DG  B  2 6   ? 38.772  81.173  117.260 1.00 29.44 ? 10   DG  I N7    1 
ATOM   197   C  C5    . DG  B  2 6   ? 39.704  80.167  117.489 1.00 25.85 ? 10   DG  I C5    1 
ATOM   198   C  C6    . DG  B  2 6   ? 39.621  78.762  117.267 1.00 30.79 ? 10   DG  I C6    1 
ATOM   199   O  O6    . DG  B  2 6   ? 38.647  78.094  116.866 1.00 30.53 ? 10   DG  I O6    1 
ATOM   200   N  N1    . DG  B  2 6   ? 40.819  78.124  117.579 1.00 27.63 ? 10   DG  I N1    1 
ATOM   201   C  C2    . DG  B  2 6   ? 41.940  78.752  118.065 1.00 31.97 ? 10   DG  I C2    1 
ATOM   202   N  N2    . DG  B  2 6   ? 43.023  77.981  118.249 1.00 25.25 ? 10   DG  I N2    1 
ATOM   203   N  N3    . DG  B  2 6   ? 42.006  80.048  118.334 1.00 27.37 ? 10   DG  I N3    1 
ATOM   204   C  C4    . DG  B  2 6   ? 40.863  80.687  118.017 1.00 28.77 ? 10   DG  I C4    1 
ATOM   205   P  P     . DC  B  2 7   ? 43.919  86.243  119.449 1.00 27.67 ? 11   DC  I P     1 
ATOM   206   O  OP1   . DC  B  2 7   ? 44.633  86.996  120.518 1.00 27.31 ? 11   DC  I OP1   1 
ATOM   207   O  OP2   . DC  B  2 7   ? 43.127  86.984  118.447 1.00 32.91 ? 11   DC  I OP2   1 
ATOM   208   O  "O5'" . DC  B  2 7   ? 44.963  85.275  118.742 1.00 29.56 ? 11   DC  I "O5'" 1 
ATOM   209   C  "C5'" . DC  B  2 7   ? 45.856  84.482  119.526 1.00 35.44 ? 11   DC  I "C5'" 1 
ATOM   210   C  "C4'" . DC  B  2 7   ? 46.713  83.600  118.647 1.00 42.09 ? 11   DC  I "C4'" 1 
ATOM   211   O  "O4'" . DC  B  2 7   ? 45.903  82.552  118.065 1.00 41.92 ? 11   DC  I "O4'" 1 
ATOM   212   C  "C3'" . DC  B  2 7   ? 47.411  84.298  117.479 1.00 44.15 ? 11   DC  I "C3'" 1 
ATOM   213   O  "O3'" . DC  B  2 7   ? 48.648  83.643  117.180 1.00 50.64 ? 11   DC  I "O3'" 1 
ATOM   214   C  "C2'" . DC  B  2 7   ? 46.501  83.983  116.309 1.00 42.50 ? 11   DC  I "C2'" 1 
ATOM   215   C  "C1'" . DC  B  2 7   ? 46.005  82.584  116.649 1.00 41.45 ? 11   DC  I "C1'" 1 
ATOM   216   N  N1    . DC  B  2 7   ? 44.673  82.291  116.101 1.00 38.14 ? 11   DC  I N1    1 
ATOM   217   C  C2    . DC  B  2 7   ? 44.340  80.969  115.753 1.00 38.48 ? 11   DC  I C2    1 
ATOM   218   O  O2    . DC  B  2 7   ? 45.183  80.069  115.918 1.00 38.93 ? 11   DC  I O2    1 
ATOM   219   N  N3    . DC  B  2 7   ? 43.111  80.717  115.239 1.00 35.55 ? 11   DC  I N3    1 
ATOM   220   C  C4    . DC  B  2 7   ? 42.242  81.721  115.064 1.00 36.52 ? 11   DC  I C4    1 
ATOM   221   N  N4    . DC  B  2 7   ? 41.044  81.443  114.551 1.00 37.56 ? 11   DC  I N4    1 
ATOM   222   C  C5    . DC  B  2 7   ? 42.560  83.061  115.409 1.00 35.55 ? 11   DC  I C5    1 
ATOM   223   C  C6    . DC  B  2 7   ? 43.768  83.299  115.924 1.00 39.88 ? 11   DC  I C6    1 
ATOM   224   O  "O5'" . DT  C  1 1   ? 37.400  78.146  108.281 1.00 56.83 ? 1    DT  F "O5'" 1 
ATOM   225   C  "C5'" . DT  C  1 1   ? 37.410  77.162  107.235 1.00 57.27 ? 1    DT  F "C5'" 1 
ATOM   226   C  "C4'" . DT  C  1 1   ? 38.380  76.025  107.473 1.00 55.62 ? 1    DT  F "C4'" 1 
ATOM   227   O  "O4'" . DT  C  1 1   ? 39.689  76.561  107.787 1.00 53.16 ? 1    DT  F "O4'" 1 
ATOM   228   C  "C3'" . DT  C  1 1   ? 38.011  75.102  108.639 1.00 56.84 ? 1    DT  F "C3'" 1 
ATOM   229   O  "O3'" . DT  C  1 1   ? 38.340  73.744  108.329 1.00 58.94 ? 1    DT  F "O3'" 1 
ATOM   230   C  "C2'" . DT  C  1 1   ? 38.903  75.586  109.765 1.00 55.54 ? 1    DT  F "C2'" 1 
ATOM   231   C  "C1'" . DT  C  1 1   ? 40.150  75.995  109.008 1.00 53.02 ? 1    DT  F "C1'" 1 
ATOM   232   N  N1    . DT  C  1 1   ? 40.959  77.000  109.715 1.00 49.48 ? 1    DT  F N1    1 
ATOM   233   C  C2    . DT  C  1 1   ? 42.252  76.668  110.042 1.00 47.27 ? 1    DT  F C2    1 
ATOM   234   O  O2    . DT  C  1 1   ? 42.752  75.589  109.764 1.00 50.12 ? 1    DT  F O2    1 
ATOM   235   N  N3    . DT  C  1 1   ? 42.944  77.643  110.714 1.00 47.12 ? 1    DT  F N3    1 
ATOM   236   C  C4    . DT  C  1 1   ? 42.486  78.896  111.073 1.00 47.76 ? 1    DT  F C4    1 
ATOM   237   O  O4    . DT  C  1 1   ? 43.230  79.669  111.669 1.00 47.19 ? 1    DT  F O4    1 
ATOM   238   C  C5    . DT  C  1 1   ? 41.116  79.179  110.695 1.00 49.80 ? 1    DT  F C5    1 
ATOM   239   C  C7    . DT  C  1 1   ? 40.527  80.512  111.045 1.00 49.30 ? 1    DT  F C7    1 
ATOM   240   C  C6    . DT  C  1 1   ? 40.431  78.231  110.040 1.00 48.58 ? 1    DT  F C6    1 
ATOM   241   P  P     . DG  C  1 2   ? 37.792  72.555  109.271 1.00 60.04 ? 2    DG  F P     1 
ATOM   242   O  OP1   . DG  C  1 2   ? 37.595  71.380  108.388 1.00 60.04 ? 2    DG  F OP1   1 
ATOM   243   O  OP2   . DG  C  1 2   ? 36.652  73.063  110.093 1.00 57.85 ? 2    DG  F OP2   1 
ATOM   244   O  "O5'" . DG  C  1 2   ? 39.013  72.242  110.251 1.00 57.92 ? 2    DG  F "O5'" 1 
ATOM   245   C  "C5'" . DG  C  1 2   ? 40.288  71.912  109.716 1.00 54.00 ? 2    DG  F "C5'" 1 
ATOM   246   C  "C4'" . DG  C  1 2   ? 41.362  72.079  110.765 1.00 55.16 ? 2    DG  F "C4'" 1 
ATOM   247   O  "O4'" . DG  C  1 2   ? 41.367  73.417  111.314 1.00 51.83 ? 2    DG  F "O4'" 1 
ATOM   248   C  "C3'" . DG  C  1 2   ? 41.276  71.156  111.971 1.00 54.89 ? 2    DG  F "C3'" 1 
ATOM   249   O  "O3'" . DG  C  1 2   ? 42.621  70.914  112.357 1.00 56.97 ? 2    DG  F "O3'" 1 
ATOM   250   C  "C2'" . DG  C  1 2   ? 40.588  72.012  113.021 1.00 51.38 ? 2    DG  F "C2'" 1 
ATOM   251   C  "C1'" . DG  C  1 2   ? 41.208  73.361  112.731 1.00 50.11 ? 2    DG  F "C1'" 1 
ATOM   252   N  N9    . DG  C  1 2   ? 40.432  74.535  113.113 1.00 47.80 ? 2    DG  F N9    1 
ATOM   253   C  C8    . DG  C  1 2   ? 39.089  74.759  112.931 1.00 46.97 ? 2    DG  F C8    1 
ATOM   254   N  N7    . DG  C  1 2   ? 38.732  75.985  113.209 1.00 47.15 ? 2    DG  F N7    1 
ATOM   255   C  C5    . DG  C  1 2   ? 39.912  76.588  113.637 1.00 45.03 ? 2    DG  F C5    1 
ATOM   256   C  C6    . DG  C  1 2   ? 40.170  77.923  114.027 1.00 41.67 ? 2    DG  F C6    1 
ATOM   257   O  O6    . DG  C  1 2   ? 39.393  78.887  114.043 1.00 42.57 ? 2    DG  F O6    1 
ATOM   258   N  N1    . DG  C  1 2   ? 41.500  78.089  114.407 1.00 36.12 ? 2    DG  F N1    1 
ATOM   259   C  C2    . DG  C  1 2   ? 42.456  77.107  114.394 1.00 34.82 ? 2    DG  F C2    1 
ATOM   260   N  N2    . DG  C  1 2   ? 43.677  77.446  114.807 1.00 32.37 ? 2    DG  F N2    1 
ATOM   261   N  N3    . DG  C  1 2   ? 42.231  75.869  114.001 1.00 41.73 ? 2    DG  F N3    1 
ATOM   262   C  C4    . DG  C  1 2   ? 40.949  75.684  113.635 1.00 44.60 ? 2    DG  F C4    1 
ATOM   263   P  P     . DC  C  1 3   ? 42.981  69.614  113.195 1.00 55.59 ? 3    DC  F P     1 
ATOM   264   O  OP1   . DC  C  1 3   ? 44.011  68.848  112.436 1.00 59.34 ? 3    DC  F OP1   1 
ATOM   265   O  OP2   . DC  C  1 3   ? 41.710  68.956  113.596 1.00 52.83 ? 3    DC  F OP2   1 
ATOM   266   O  "O5'" . DC  C  1 3   ? 43.679  70.224  114.476 1.00 49.55 ? 3    DC  F "O5'" 1 
ATOM   267   C  "C5'" . DC  C  1 3   ? 44.751  71.144  114.336 1.00 39.55 ? 3    DC  F "C5'" 1 
ATOM   268   C  "C4'" . DC  C  1 3   ? 44.990  71.819  115.659 1.00 36.88 ? 3    DC  F "C4'" 1 
ATOM   269   O  "O4'" . DC  C  1 3   ? 44.017  72.864  115.885 1.00 37.88 ? 3    DC  F "O4'" 1 
ATOM   270   C  "C3'" . DC  C  1 3   ? 44.795  70.837  116.810 1.00 33.35 ? 3    DC  F "C3'" 1 
ATOM   271   O  "O3'" . DC  C  1 3   ? 45.720  71.167  117.818 1.00 32.49 ? 3    DC  F "O3'" 1 
ATOM   272   C  "C2'" . DC  C  1 3   ? 43.394  71.137  117.305 1.00 32.10 ? 3    DC  F "C2'" 1 
ATOM   273   C  "C1'" . DC  C  1 3   ? 43.380  72.627  117.134 1.00 32.46 ? 3    DC  F "C1'" 1 
ATOM   274   N  N1    . DC  C  1 3   ? 42.063  73.266  117.089 1.00 31.53 ? 3    DC  F N1    1 
ATOM   275   C  C2    . DC  C  1 3   ? 42.019  74.622  117.306 1.00 32.44 ? 3    DC  F C2    1 
ATOM   276   O  O2    . DC  C  1 3   ? 43.083  75.209  117.547 1.00 29.87 ? 3    DC  F O2    1 
ATOM   277   N  N3    . DC  C  1 3   ? 40.833  75.270  117.246 1.00 32.29 ? 3    DC  F N3    1 
ATOM   278   C  C4    . DC  C  1 3   ? 39.720  74.594  116.983 1.00 33.89 ? 3    DC  F C4    1 
ATOM   279   N  N4    . DC  C  1 3   ? 38.574  75.282  116.921 1.00 34.83 ? 3    DC  F N4    1 
ATOM   280   C  C5    . DC  C  1 3   ? 39.731  73.182  116.769 1.00 37.00 ? 3    DC  F C5    1 
ATOM   281   C  C6    . DC  C  1 3   ? 40.921  72.562  116.832 1.00 34.63 ? 3    DC  F C6    1 
ATOM   282   P  P     . DG  C  1 4   ? 47.056  70.321  117.942 1.00 31.85 ? 4    DG  F P     1 
ATOM   283   O  OP1   . DG  C  1 4   ? 47.735  70.347  116.626 1.00 28.18 ? 4    DG  F OP1   1 
ATOM   284   O  OP2   . DG  C  1 4   ? 46.708  69.003  118.569 1.00 34.98 ? 4    DG  F OP2   1 
ATOM   285   O  "O5'" . DG  C  1 4   ? 47.913  71.181  118.978 1.00 33.00 ? 4    DG  F "O5'" 1 
ATOM   286   C  "C5'" . DG  C  1 4   ? 48.514  72.427  118.578 1.00 29.36 ? 4    DG  F "C5'" 1 
ATOM   287   C  "C4'" . DG  C  1 4   ? 48.460  73.431  119.706 1.00 28.24 ? 4    DG  F "C4'" 1 
ATOM   288   O  "O4'" . DG  C  1 4   ? 47.086  73.827  119.945 1.00 30.01 ? 4    DG  F "O4'" 1 
ATOM   289   C  "C3'" . DG  C  1 4   ? 48.991  72.951  121.054 1.00 23.56 ? 4    DG  F "C3'" 1 
ATOM   290   O  "O3'" . DG  C  1 4   ? 49.429  74.145  121.699 1.00 23.37 ? 4    DG  F "O3'" 1 
ATOM   291   C  "C2'" . DG  C  1 4   ? 47.728  72.508  121.773 1.00 27.16 ? 4    DG  F "C2'" 1 
ATOM   292   C  "C1'" . DG  C  1 4   ? 46.707  73.517  121.288 1.00 26.28 ? 4    DG  F "C1'" 1 
ATOM   293   N  N9    . DG  C  1 4   ? 45.344  73.013  121.212 1.00 19.43 ? 4    DG  F N9    1 
ATOM   294   C  C8    . DG  C  1 4   ? 44.948  71.702  121.096 1.00 18.93 ? 4    DG  F C8    1 
ATOM   295   N  N7    . DG  C  1 4   ? 43.668  71.573  120.910 1.00 20.99 ? 4    DG  F N7    1 
ATOM   296   C  C5    . DG  C  1 4   ? 43.189  72.878  120.919 1.00 18.61 ? 4    DG  F C5    1 
ATOM   297   C  C6    . DG  C  1 4   ? 41.876  73.374  120.730 1.00 20.16 ? 4    DG  F C6    1 
ATOM   298   O  O6    . DG  C  1 4   ? 40.847  72.748  120.457 1.00 21.39 ? 4    DG  F O6    1 
ATOM   299   N  N1    . DG  C  1 4   ? 41.830  74.760  120.865 1.00 20.87 ? 4    DG  F N1    1 
ATOM   300   C  C2    . DG  C  1 4   ? 42.917  75.564  121.126 1.00 18.95 ? 4    DG  F C2    1 
ATOM   301   N  N2    . DG  C  1 4   ? 42.666  76.885  121.253 1.00 21.22 ? 4    DG  F N2    1 
ATOM   302   N  N3    . DG  C  1 4   ? 44.154  75.116  121.265 1.00 16.98 ? 4    DG  F N3    1 
ATOM   303   C  C4    . DG  C  1 4   ? 44.211  73.772  121.155 1.00 17.73 ? 4    DG  F C4    1 
ATOM   304   O  OP3   . DC  D  2 1   ? 50.162  73.426  123.982 1.00 25.96 ? 5    DC  J OP3   1 
ATOM   305   P  P     . DC  D  2 1   ? 50.232  74.339  125.183 1.00 20.28 ? 5    DC  J P     1 
ATOM   306   O  OP1   . DC  D  2 1   ? 49.871  73.657  126.491 1.00 18.38 ? 5    DC  J OP1   1 
ATOM   307   O  OP2   . DC  D  2 1   ? 51.509  75.143  125.253 1.00 21.20 ? 5    DC  J OP2   1 
ATOM   308   O  "O5'" . DC  D  2 1   ? 49.059  75.452  124.972 1.00 19.60 ? 5    DC  J "O5'" 1 
ATOM   309   C  "C5'" . DC  D  2 1   ? 49.348  76.698  124.337 1.00 22.85 ? 5    DC  J "C5'" 1 
ATOM   310   C  "C4'" . DC  D  2 1   ? 48.230  77.680  124.586 1.00 16.73 ? 5    DC  J "C4'" 1 
ATOM   311   O  "O4'" . DC  D  2 1   ? 47.087  77.273  123.786 1.00 19.16 ? 5    DC  J "O4'" 1 
ATOM   312   C  "C3'" . DC  D  2 1   ? 47.723  77.699  126.023 1.00 18.24 ? 5    DC  J "C3'" 1 
ATOM   313   O  "O3'" . DC  D  2 1   ? 48.334  78.718  126.776 1.00 15.70 ? 5    DC  J "O3'" 1 
ATOM   314   C  "C2'" . DC  D  2 1   ? 46.223  77.939  125.897 1.00 28.29 ? 5    DC  J "C2'" 1 
ATOM   315   C  "C1'" . DC  D  2 1   ? 45.862  77.530  124.485 1.00 21.20 ? 5    DC  J "C1'" 1 
ATOM   316   N  N1    . DC  D  2 1   ? 45.091  76.262  124.515 1.00 19.37 ? 5    DC  J N1    1 
ATOM   317   C  C2    . DC  D  2 1   ? 43.704  76.325  124.530 1.00 19.62 ? 5    DC  J C2    1 
ATOM   318   O  O2    . DC  D  2 1   ? 43.168  77.434  124.574 1.00 20.25 ? 5    DC  J O2    1 
ATOM   319   N  N3    . DC  D  2 1   ? 42.978  75.170  124.502 1.00 18.16 ? 5    DC  J N3    1 
ATOM   320   C  C4    . DC  D  2 1   ? 43.603  73.990  124.487 1.00 17.73 ? 5    DC  J C4    1 
ATOM   321   N  N4    . DC  D  2 1   ? 42.853  72.881  124.454 1.00 18.03 ? 5    DC  J N4    1 
ATOM   322   C  C5    . DC  D  2 1   ? 45.029  73.894  124.501 1.00 17.94 ? 5    DC  J C5    1 
ATOM   323   C  C6    . DC  D  2 1   ? 45.726  75.046  124.519 1.00 18.01 ? 5    DC  J C6    1 
ATOM   324   P  P     . DC  D  2 2   ? 48.433  78.565  128.368 1.00 17.42 ? 6    DC  J P     1 
ATOM   325   O  OP1   . DC  D  2 2   ? 49.350  79.615  128.834 1.00 15.93 ? 6    DC  J OP1   1 
ATOM   326   O  OP2   . DC  D  2 2   ? 48.656  77.147  128.771 1.00 19.02 ? 6    DC  J OP2   1 
ATOM   327   O  "O5'" . DC  D  2 2   ? 46.960  78.926  128.849 1.00 17.21 ? 6    DC  J "O5'" 1 
ATOM   328   C  "C5'" . DC  D  2 2   ? 46.425  80.203  128.547 1.00 17.50 ? 6    DC  J "C5'" 1 
ATOM   329   C  "C4'" . DC  D  2 2   ? 45.007  80.324  129.058 1.00 15.94 ? 6    DC  J "C4'" 1 
ATOM   330   O  "O4'" . DC  D  2 2   ? 44.142  79.391  128.380 1.00 16.12 ? 6    DC  J "O4'" 1 
ATOM   331   C  "C3'" . DC  D  2 2   ? 44.809  80.114  130.564 1.00 20.28 ? 6    DC  J "C3'" 1 
ATOM   332   O  "O3'" . DC  D  2 2   ? 44.120  81.303  131.034 1.00 24.66 ? 6    DC  J "O3'" 1 
ATOM   333   C  "C2'" . DC  D  2 2   ? 44.092  78.769  130.653 1.00 18.21 ? 6    DC  J "C2'" 1 
ATOM   334   C  "C1'" . DC  D  2 2   ? 43.377  78.636  129.318 1.00 16.59 ? 6    DC  J "C1'" 1 
ATOM   335   N  N1    . DC  D  2 2   ? 43.288  77.258  128.809 1.00 18.42 ? 6    DC  J N1    1 
ATOM   336   C  C2    . DC  D  2 2   ? 42.022  76.656  128.653 1.00 22.24 ? 6    DC  J C2    1 
ATOM   337   O  O2    . DC  D  2 2   ? 40.984  77.352  128.880 1.00 19.42 ? 6    DC  J O2    1 
ATOM   338   N  N3    . DC  D  2 2   ? 41.947  75.351  128.254 1.00 15.77 ? 6    DC  J N3    1 
ATOM   339   C  C4    . DC  D  2 2   ? 43.081  74.660  127.985 1.00 16.37 ? 6    DC  J C4    1 
ATOM   340   N  N4    . DC  D  2 2   ? 42.969  73.360  127.611 1.00 16.92 ? 6    DC  J N4    1 
ATOM   341   C  C5    . DC  D  2 2   ? 44.366  75.264  128.083 1.00 16.87 ? 6    DC  J C5    1 
ATOM   342   C  C6    . DC  D  2 2   ? 44.432  76.555  128.502 1.00 17.83 ? 6    DC  J C6    1 
ATOM   343   P  P     . DG  D  2 3   ? 42.999  81.266  132.200 1.00 21.18 ? 7    DG  J P     1 
ATOM   344   O  OP1   . DG  D  2 3   ? 42.713  82.702  132.390 1.00 22.00 ? 7    DG  J OP1   1 
ATOM   345   O  OP2   . DG  D  2 3   ? 43.376  80.434  133.386 1.00 21.52 ? 7    DG  J OP2   1 
ATOM   346   O  "O5'" . DG  D  2 3   ? 41.749  80.549  131.541 1.00 19.32 ? 7    DG  J "O5'" 1 
ATOM   347   C  "C5'" . DG  D  2 3   ? 40.867  81.231  130.657 1.00 22.34 ? 7    DG  J "C5'" 1 
ATOM   348   C  "C4'" . DG  D  2 3   ? 39.439  81.048  131.122 1.00 20.41 ? 7    DG  J "C4'" 1 
ATOM   349   O  "O4'" . DG  D  2 3   ? 39.044  79.666  130.990 1.00 20.24 ? 7    DG  J "O4'" 1 
ATOM   350   C  "C3'" . DG  D  2 3   ? 39.199  81.409  132.584 1.00 21.59 ? 7    DG  J "C3'" 1 
ATOM   351   O  "O3'" . DG  D  2 3   ? 37.923  82.047  132.681 1.00 24.73 ? 7    DG  J "O3'" 1 
ATOM   352   C  "C2'" . DG  D  2 3   ? 39.299  80.077  133.312 1.00 22.80 ? 7    DG  J "C2'" 1 
ATOM   353   C  "C1'" . DG  D  2 3   ? 38.887  79.050  132.265 1.00 18.76 ? 7    DG  J "C1'" 1 
ATOM   354   N  N9    . DG  D  2 3   ? 39.727  77.853  132.281 1.00 19.57 ? 7    DG  J N9    1 
ATOM   355   C  C8    . DG  D  2 3   ? 41.049  77.771  132.654 1.00 20.22 ? 7    DG  J C8    1 
ATOM   356   N  N7    . DG  D  2 3   ? 41.534  76.556  132.577 1.00 18.46 ? 7    DG  J N7    1 
ATOM   357   C  C5    . DG  D  2 3   ? 40.471  75.793  132.111 1.00 17.57 ? 7    DG  J C5    1 
ATOM   358   C  C6    . DG  D  2 3   ? 40.390  74.405  131.816 1.00 18.76 ? 7    DG  J C6    1 
ATOM   359   O  O6    . DG  D  2 3   ? 41.281  73.555  131.876 1.00 17.60 ? 7    DG  J O6    1 
ATOM   360   N  N1    . DG  D  2 3   ? 39.112  74.041  131.396 1.00 18.13 ? 7    DG  J N1    1 
ATOM   361   C  C2    . DG  D  2 3   ? 38.048  74.922  131.242 1.00 20.21 ? 7    DG  J C2    1 
ATOM   362   N  N2    . DG  D  2 3   ? 36.886  74.396  130.818 1.00 17.77 ? 7    DG  J N2    1 
ATOM   363   N  N3    . DG  D  2 3   ? 38.124  76.215  131.487 1.00 18.90 ? 7    DG  J N3    1 
ATOM   364   C  C4    . DG  D  2 3   ? 39.347  76.580  131.928 1.00 19.00 ? 7    DG  J C4    1 
ATOM   365   P  P     . DG  D  2 4   ? 37.221  82.242  134.104 1.00 25.64 ? 8    DG  J P     1 
ATOM   366   O  OP1   . DG  D  2 4   ? 36.440  83.504  133.979 1.00 31.54 ? 8    DG  J OP1   1 
ATOM   367   O  OP2   . DG  D  2 4   ? 38.153  82.066  135.235 1.00 27.75 ? 8    DG  J OP2   1 
ATOM   368   O  "O5'" . DG  D  2 4   ? 36.190  81.040  134.117 1.00 21.19 ? 8    DG  J "O5'" 1 
ATOM   369   C  "C5'" . DG  D  2 4   ? 35.347  80.834  132.992 1.00 20.33 ? 8    DG  J "C5'" 1 
ATOM   370   C  "C4'" . DG  D  2 4   ? 34.458  79.636  133.222 1.00 21.70 ? 8    DG  J "C4'" 1 
ATOM   371   O  "O4'" . DG  D  2 4   ? 35.255  78.418  133.197 1.00 22.90 ? 8    DG  J "O4'" 1 
ATOM   372   C  "C3'" . DG  D  2 4   ? 33.693  79.633  134.550 1.00 21.37 ? 8    DG  J "C3'" 1 
ATOM   373   O  "O3'" . DG  D  2 4   ? 32.357  79.202  134.270 1.00 22.08 ? 8    DG  J "O3'" 1 
ATOM   374   C  "C2'" . DG  D  2 4   ? 34.450  78.613  135.395 1.00 19.20 ? 8    DG  J "C2'" 1 
ATOM   375   C  "C1'" . DG  D  2 4   ? 34.965  77.630  134.348 1.00 19.63 ? 8    DG  J "C1'" 1 
ATOM   376   N  N9    . DG  D  2 4   ? 36.201  76.955  134.730 1.00 17.86 ? 8    DG  J N9    1 
ATOM   377   C  C8    . DG  D  2 4   ? 37.335  77.546  135.238 1.00 19.90 ? 8    DG  J C8    1 
ATOM   378   N  N7    . DG  D  2 4   ? 38.302  76.694  135.453 1.00 20.23 ? 8    DG  J N7    1 
ATOM   379   C  C5    . DG  D  2 4   ? 37.772  75.470  135.073 1.00 18.48 ? 8    DG  J C5    1 
ATOM   380   C  C6    . DG  D  2 4   ? 38.350  74.177  135.094 1.00 18.96 ? 8    DG  J C6    1 
ATOM   381   O  O6    . DG  D  2 4   ? 39.491  73.859  135.440 1.00 21.13 ? 8    DG  J O6    1 
ATOM   382   N  N1    . DG  D  2 4   ? 37.458  73.204  134.647 1.00 18.81 ? 8    DG  J N1    1 
ATOM   383   C  C2    . DG  D  2 4   ? 36.190  73.444  134.211 1.00 20.37 ? 8    DG  J C2    1 
ATOM   384   N  N2    . DG  D  2 4   ? 35.495  72.366  133.778 1.00 17.06 ? 8    DG  J N2    1 
ATOM   385   N  N3    . DG  D  2 4   ? 35.635  74.660  134.188 1.00 18.60 ? 8    DG  J N3    1 
ATOM   386   C  C4    . DG  D  2 4   ? 36.474  75.613  134.635 1.00 17.95 ? 8    DG  J C4    1 
ATOM   387   P  P     . DC  D  2 5   ? 31.200  79.305  135.388 1.00 20.59 ? 9    DC  J P     1 
ATOM   388   O  OP1   . DC  D  2 5   ? 29.941  79.330  134.630 1.00 22.06 ? 9    DC  J OP1   1 
ATOM   389   O  OP2   . DC  D  2 5   ? 31.493  80.351  136.383 1.00 22.74 ? 9    DC  J OP2   1 
ATOM   390   O  "O5'" . DC  D  2 5   ? 31.322  77.929  136.171 1.00 17.96 ? 9    DC  J "O5'" 1 
ATOM   391   C  "C5'" . DC  D  2 5   ? 31.034  76.697  135.531 1.00 19.34 ? 9    DC  J "C5'" 1 
ATOM   392   C  "C4'" . DC  D  2 5   ? 31.289  75.555  136.486 1.00 18.97 ? 9    DC  J "C4'" 1 
ATOM   393   O  "O4'" . DC  D  2 5   ? 32.710  75.323  136.613 1.00 18.87 ? 9    DC  J "O4'" 1 
ATOM   394   C  "C3'" . DC  D  2 5   ? 30.773  75.794  137.910 1.00 18.53 ? 9    DC  J "C3'" 1 
ATOM   395   O  "O3'" . DC  D  2 5   ? 30.090  74.620  138.355 1.00 21.50 ? 9    DC  J "O3'" 1 
ATOM   396   C  "C2'" . DC  D  2 5   ? 32.034  75.965  138.735 1.00 20.19 ? 9    DC  J "C2'" 1 
ATOM   397   C  "C1'" . DC  D  2 5   ? 33.001  75.070  137.979 1.00 17.84 ? 9    DC  J "C1'" 1 
ATOM   398   N  N1    . DC  D  2 5   ? 34.428  75.321  138.190 1.00 18.52 ? 9    DC  J N1    1 
ATOM   399   C  C2    . DC  D  2 5   ? 35.322  74.218  138.158 1.00 17.58 ? 9    DC  J C2    1 
ATOM   400   O  O2    . DC  D  2 5   ? 34.866  73.082  137.962 1.00 17.79 ? 9    DC  J O2    1 
ATOM   401   N  N3    . DC  D  2 5   ? 36.643  74.436  138.337 1.00 17.00 ? 9    DC  J N3    1 
ATOM   402   C  C4    . DC  D  2 5   ? 37.098  75.687  138.526 1.00 20.56 ? 9    DC  J C4    1 
ATOM   403   N  N4    . DC  D  2 5   ? 38.419  75.862  138.682 1.00 19.68 ? 9    DC  J N4    1 
ATOM   404   C  C5    . DC  D  2 5   ? 36.216  76.817  138.562 1.00 20.28 ? 9    DC  J C5    1 
ATOM   405   C  C6    . DC  D  2 5   ? 34.904  76.585  138.400 1.00 20.21 ? 9    DC  J C6    1 
ATOM   406   P  P     . DG  D  2 6   ? 28.492  74.528  138.228 1.00 21.26 ? 10   DG  J P     1 
ATOM   407   O  OP1   . DG  D  2 6   ? 28.029  75.021  136.899 1.00 20.77 ? 10   DG  J OP1   1 
ATOM   408   O  OP2   . DG  D  2 6   ? 27.939  75.147  139.481 1.00 25.03 ? 10   DG  J OP2   1 
ATOM   409   O  "O5'" . DG  D  2 6   ? 28.232  72.967  138.291 1.00 23.13 ? 10   DG  J "O5'" 1 
ATOM   410   C  "C5'" . DG  D  2 6   ? 28.502  72.139  137.158 1.00 21.91 ? 10   DG  J "C5'" 1 
ATOM   411   C  "C4'" . DG  D  2 6   ? 29.023  70.792  137.606 1.00 24.27 ? 10   DG  J "C4'" 1 
ATOM   412   O  "O4'" . DG  D  2 6   ? 30.304  70.920  138.257 1.00 24.72 ? 10   DG  J "O4'" 1 
ATOM   413   C  "C3'" . DG  D  2 6   ? 28.144  70.027  138.587 1.00 25.48 ? 10   DG  J "C3'" 1 
ATOM   414   O  "O3'" . DG  D  2 6   ? 28.333  68.650  138.272 1.00 26.73 ? 10   DG  J "O3'" 1 
ATOM   415   C  "C2'" . DG  D  2 6   ? 28.731  70.388  139.942 1.00 25.99 ? 10   DG  J "C2'" 1 
ATOM   416   C  "C1'" . DG  D  2 6   ? 30.217  70.558  139.631 1.00 24.68 ? 10   DG  J "C1'" 1 
ATOM   417   N  N9    . DG  D  2 6   ? 30.893  71.624  140.355 1.00 25.55 ? 10   DG  J N9    1 
ATOM   418   C  C8    . DG  D  2 6   ? 30.355  72.820  140.758 1.00 23.36 ? 10   DG  J C8    1 
ATOM   419   N  N7    . DG  D  2 6   ? 31.249  73.650  141.220 1.00 26.69 ? 10   DG  J N7    1 
ATOM   420   C  C5    . DG  D  2 6   ? 32.442  72.943  141.153 1.00 21.52 ? 10   DG  J C5    1 
ATOM   421   C  C6    . DG  D  2 6   ? 33.765  73.338  141.482 1.00 24.13 ? 10   DG  J C6    1 
ATOM   422   O  O6    . DG  D  2 6   ? 34.170  74.445  141.852 1.00 24.82 ? 10   DG  J O6    1 
ATOM   423   N  N1    . DG  D  2 6   ? 34.669  72.293  141.314 1.00 25.54 ? 10   DG  J N1    1 
ATOM   424   C  C2    . DG  D  2 6   ? 34.345  71.042  140.864 1.00 23.73 ? 10   DG  J C2    1 
ATOM   425   N  N2    . DG  D  2 6   ? 35.343  70.160  140.819 1.00 22.11 ? 10   DG  J N2    1 
ATOM   426   N  N3    . DG  D  2 6   ? 33.125  70.678  140.495 1.00 21.59 ? 10   DG  J N3    1 
ATOM   427   C  C4    . DG  D  2 6   ? 32.230  71.672  140.670 1.00 22.40 ? 10   DG  J C4    1 
ATOM   428   P  P     . DC  D  2 7   ? 27.453  67.518  138.984 1.00 27.60 ? 11   DC  J P     1 
ATOM   429   O  OP1   . DC  D  2 7   ? 26.903  66.670  137.900 1.00 30.66 ? 11   DC  J OP1   1 
ATOM   430   O  OP2   . DC  D  2 7   ? 26.528  68.145  139.964 1.00 30.73 ? 11   DC  J OP2   1 
ATOM   431   O  "O5'" . DC  D  2 7   ? 28.548  66.682  139.782 1.00 31.14 ? 11   DC  J "O5'" 1 
ATOM   432   C  "C5'" . DC  D  2 7   ? 29.655  66.089  139.090 1.00 31.65 ? 11   DC  J "C5'" 1 
ATOM   433   C  "C4'" . DC  D  2 7   ? 30.537  65.331  140.057 1.00 35.04 ? 11   DC  J "C4'" 1 
ATOM   434   O  "O4'" . DC  D  2 7   ? 31.197  66.270  140.938 1.00 33.63 ? 11   DC  J "O4'" 1 
ATOM   435   C  "C3'" . DC  D  2 7   ? 29.795  64.357  140.969 1.00 34.73 ? 11   DC  J "C3'" 1 
ATOM   436   O  "O3'" . DC  D  2 7   ? 30.673  63.296  141.346 1.00 41.86 ? 11   DC  J "O3'" 1 
ATOM   437   C  "C2'" . DC  D  2 7   ? 29.505  65.207  142.196 1.00 36.07 ? 11   DC  J "C2'" 1 
ATOM   438   C  "C1'" . DC  D  2 7   ? 30.730  66.112  142.271 1.00 34.79 ? 11   DC  J "C1'" 1 
ATOM   439   N  N1    . DC  D  2 7   ? 30.504  67.465  142.801 1.00 35.85 ? 11   DC  J N1    1 
ATOM   440   C  C2    . DC  D  2 7   ? 31.612  68.213  143.176 1.00 35.05 ? 11   DC  J C2    1 
ATOM   441   O  O2    . DC  D  2 7   ? 32.728  67.677  143.151 1.00 38.85 ? 11   DC  J O2    1 
ATOM   442   N  N3    . DC  D  2 7   ? 31.447  69.495  143.567 1.00 33.26 ? 11   DC  J N3    1 
ATOM   443   C  C4    . DC  D  2 7   ? 30.227  70.023  143.612 1.00 31.52 ? 11   DC  J C4    1 
ATOM   444   N  N4    . DC  D  2 7   ? 30.115  71.310  143.978 1.00 33.80 ? 11   DC  J N4    1 
ATOM   445   C  C5    . DC  D  2 7   ? 29.068  69.264  143.285 1.00 35.95 ? 11   DC  J C5    1 
ATOM   446   C  C6    . DC  D  2 7   ? 29.250  67.998  142.890 1.00 35.96 ? 11   DC  J C6    1 
ATOM   447   O  "O5'" . DT  E  1 1   ? 81.743  31.525  108.267 1.00 43.63 ? 1    DT  G "O5'" 1 
ATOM   448   C  "C5'" . DT  E  1 1   ? 82.336  32.120  109.420 1.00 51.55 ? 1    DT  G "C5'" 1 
ATOM   449   C  "C4'" . DT  E  1 1   ? 81.339  32.488  110.496 1.00 49.40 ? 1    DT  G "C4'" 1 
ATOM   450   O  "O4'" . DT  E  1 1   ? 81.064  31.366  111.379 1.00 49.15 ? 1    DT  G "O4'" 1 
ATOM   451   C  "C3'" . DT  E  1 1   ? 81.814  33.626  111.399 1.00 51.04 ? 1    DT  G "C3'" 1 
ATOM   452   O  "O3'" . DT  E  1 1   ? 80.744  34.556  111.562 1.00 50.96 ? 1    DT  G "O3'" 1 
ATOM   453   C  "C2'" . DT  E  1 1   ? 82.144  32.933  112.713 1.00 51.79 ? 1    DT  G "C2'" 1 
ATOM   454   C  "C1'" . DT  E  1 1   ? 81.106  31.834  112.720 1.00 51.66 ? 1    DT  G "C1'" 1 
ATOM   455   N  N1    . DT  E  1 1   ? 81.335  30.688  113.633 1.00 51.82 ? 1    DT  G N1    1 
ATOM   456   C  C2    . DT  E  1 1   ? 80.240  29.900  113.920 1.00 54.92 ? 1    DT  G C2    1 
ATOM   457   O  O2    . DT  E  1 1   ? 79.135  30.099  113.438 1.00 60.03 ? 1    DT  G O2    1 
ATOM   458   N  N3    . DT  E  1 1   ? 80.477  28.871  114.795 1.00 56.36 ? 1    DT  G N3    1 
ATOM   459   C  C4    . DT  E  1 1   ? 81.674  28.546  115.399 1.00 52.92 ? 1    DT  G C4    1 
ATOM   460   O  O4    . DT  E  1 1   ? 81.729  27.582  116.164 1.00 54.65 ? 1    DT  G O4    1 
ATOM   461   C  C5    . DT  E  1 1   ? 82.790  29.408  115.056 1.00 52.40 ? 1    DT  G C5    1 
ATOM   462   C  C7    . DT  E  1 1   ? 84.126  29.137  115.680 1.00 48.51 ? 1    DT  G C7    1 
ATOM   463   C  C6    . DT  E  1 1   ? 82.575  30.420  114.193 1.00 53.50 ? 1    DT  G C6    1 
ATOM   464   P  P     . DG  E  1 2   ? 81.066  36.096  111.885 1.00 51.31 ? 2    DG  G P     1 
ATOM   465   O  OP1   . DG  E  1 2   ? 80.214  36.964  111.031 1.00 48.05 ? 2    DG  G OP1   1 
ATOM   466   O  OP2   . DG  E  1 2   ? 82.543  36.258  111.854 1.00 48.66 ? 2    DG  G OP2   1 
ATOM   467   O  "O5'" . DG  E  1 2   ? 80.534  36.250  113.375 1.00 45.84 ? 2    DG  G "O5'" 1 
ATOM   468   C  "C5'" . DG  E  1 2   ? 79.132  36.202  113.630 1.00 43.54 ? 2    DG  G "C5'" 1 
ATOM   469   C  "C4'" . DG  E  1 2   ? 78.871  36.117  115.111 1.00 42.06 ? 2    DG  G "C4'" 1 
ATOM   470   O  "O4'" . DG  E  1 2   ? 79.146  34.773  115.591 1.00 42.37 ? 2    DG  G "O4'" 1 
ATOM   471   C  "C3'" . DG  E  1 2   ? 79.754  37.059  115.942 1.00 42.05 ? 2    DG  G "C3'" 1 
ATOM   472   O  "O3'" . DG  E  1 2   ? 78.991  37.579  117.034 1.00 45.22 ? 2    DG  G "O3'" 1 
ATOM   473   C  "C2'" . DG  E  1 2   ? 80.806  36.115  116.503 1.00 40.59 ? 2    DG  G "C2'" 1 
ATOM   474   C  "C1'" . DG  E  1 2   ? 79.942  34.891  116.756 1.00 37.96 ? 2    DG  G "C1'" 1 
ATOM   475   N  N9    . DG  E  1 2   ? 80.595  33.608  117.024 1.00 33.27 ? 2    DG  G N9    1 
ATOM   476   C  C8    . DG  E  1 2   ? 81.866  33.209  116.681 1.00 32.04 ? 2    DG  G C8    1 
ATOM   477   N  N7    . DG  E  1 2   ? 82.161  32.007  117.115 1.00 30.53 ? 2    DG  G N7    1 
ATOM   478   C  C5    . DG  E  1 2   ? 81.007  31.589  117.774 1.00 30.95 ? 2    DG  G C5    1 
ATOM   479   C  C6    . DG  E  1 2   ? 80.726  30.373  118.454 1.00 29.81 ? 2    DG  G C6    1 
ATOM   480   O  O6    . DG  E  1 2   ? 81.464  29.386  118.627 1.00 35.98 ? 2    DG  G O6    1 
ATOM   481   N  N1    . DG  E  1 2   ? 79.434  30.370  118.975 1.00 27.04 ? 2    DG  G N1    1 
ATOM   482   C  C2    . DG  E  1 2   ? 78.536  31.399  118.870 1.00 26.34 ? 2    DG  G C2    1 
ATOM   483   N  N2    . DG  E  1 2   ? 77.348  31.221  119.468 1.00 31.86 ? 2    DG  G N2    1 
ATOM   484   N  N3    . DG  E  1 2   ? 78.786  32.536  118.233 1.00 28.56 ? 2    DG  G N3    1 
ATOM   485   C  C4    . DG  E  1 2   ? 80.032  32.561  117.717 1.00 29.09 ? 2    DG  G C4    1 
ATOM   486   P  P     . DC  E  1 3   ? 78.382  39.073  116.975 1.00 46.91 ? 3    DC  G P     1 
ATOM   487   O  OP1   . DC  E  1 3   ? 78.044  39.406  115.563 1.00 47.08 ? 3    DC  G OP1   1 
ATOM   488   O  OP2   . DC  E  1 3   ? 79.236  40.005  117.767 1.00 44.92 ? 3    DC  G OP2   1 
ATOM   489   O  "O5'" . DC  E  1 3   ? 77.019  38.926  117.780 1.00 40.87 ? 3    DC  G "O5'" 1 
ATOM   490   C  "C5'" . DC  E  1 3   ? 75.980  38.077  117.308 1.00 39.97 ? 3    DC  G "C5'" 1 
ATOM   491   C  "C4'" . DC  E  1 3   ? 75.323  37.354  118.463 1.00 34.95 ? 3    DC  G "C4'" 1 
ATOM   492   O  "O4'" . DC  E  1 3   ? 76.139  36.250  118.918 1.00 32.19 ? 3    DC  G "O4'" 1 
ATOM   493   C  "C3'" . DC  E  1 3   ? 75.002  38.196  119.698 1.00 36.13 ? 3    DC  G "C3'" 1 
ATOM   494   O  "O3'" . DC  E  1 3   ? 73.639  37.985  120.032 1.00 34.47 ? 3    DC  G "O3'" 1 
ATOM   495   C  "C2'" . DC  E  1 3   ? 75.959  37.688  120.772 1.00 29.35 ? 3    DC  G "C2'" 1 
ATOM   496   C  "C1'" . DC  E  1 3   ? 76.281  36.264  120.333 1.00 33.33 ? 3    DC  G "C1'" 1 
ATOM   497   N  N1    . DC  E  1 3   ? 77.653  35.795  120.607 1.00 29.89 ? 3    DC  G N1    1 
ATOM   498   C  C2    . DC  E  1 3   ? 77.850  34.527  121.202 1.00 29.92 ? 3    DC  G C2    1 
ATOM   499   O  O2    . DC  E  1 3   ? 76.853  33.867  121.574 1.00 29.32 ? 3    DC  G O2    1 
ATOM   500   N  N3    . DC  E  1 3   ? 79.116  34.054  121.341 1.00 25.05 ? 3    DC  G N3    1 
ATOM   501   C  C4    . DC  E  1 3   ? 80.153  34.796  120.925 1.00 24.59 ? 3    DC  G C4    1 
ATOM   502   N  N4    . DC  E  1 3   ? 81.384  34.280  121.027 1.00 30.03 ? 3    DC  G N4    1 
ATOM   503   C  C5    . DC  E  1 3   ? 79.975  36.102  120.371 1.00 26.63 ? 3    DC  G C5    1 
ATOM   504   C  C6    . DC  E  1 3   ? 78.727  36.563  120.245 1.00 25.32 ? 3    DC  G C6    1 
ATOM   505   P  P     . DG  E  1 4   ? 72.996  38.744  121.281 1.00 42.87 ? 4    DG  G P     1 
ATOM   506   O  OP1   . DG  E  1 4   ? 71.519  38.668  121.155 1.00 48.19 ? 4    DG  G OP1   1 
ATOM   507   O  OP2   . DG  E  1 4   ? 73.660  40.073  121.451 1.00 42.29 ? 4    DG  G OP2   1 
ATOM   508   O  "O5'" . DG  E  1 4   ? 73.447  37.785  122.471 1.00 38.03 ? 4    DG  G "O5'" 1 
ATOM   509   C  "C5'" . DG  E  1 4   ? 73.176  36.386  122.376 1.00 30.19 ? 4    DG  G "C5'" 1 
ATOM   510   C  "C4'" . DG  E  1 4   ? 73.516  35.693  123.674 1.00 25.13 ? 4    DG  G "C4'" 1 
ATOM   511   O  "O4'" . DG  E  1 4   ? 74.939  35.458  123.775 1.00 24.77 ? 4    DG  G "O4'" 1 
ATOM   512   C  "C3'" . DG  E  1 4   ? 73.139  36.485  124.924 1.00 23.73 ? 4    DG  G "C3'" 1 
ATOM   513   O  "O3'" . DG  E  1 4   ? 72.920  35.483  125.920 1.00 23.27 ? 4    DG  G "O3'" 1 
ATOM   514   C  "C2'" . DG  E  1 4   ? 74.441  37.176  125.287 1.00 25.33 ? 4    DG  G "C2'" 1 
ATOM   515   C  "C1'" . DG  E  1 4   ? 75.459  36.109  124.941 1.00 21.47 ? 4    DG  G "C1'" 1 
ATOM   516   N  N9    . DG  E  1 4   ? 76.806  36.570  124.606 1.00 16.69 ? 4    DG  G N9    1 
ATOM   517   C  C8    . DG  E  1 4   ? 77.182  37.803  124.115 1.00 16.62 ? 4    DG  G C8    1 
ATOM   518   N  N7    . DG  E  1 4   ? 78.449  37.868  123.821 1.00 15.01 ? 4    DG  G N7    1 
ATOM   519   C  C5    . DG  E  1 4   ? 78.944  36.616  124.157 1.00 14.39 ? 4    DG  G C5    1 
ATOM   520   C  C6    . DG  E  1 4   ? 80.260  36.085  124.052 1.00 14.65 ? 4    DG  G C6    1 
ATOM   521   O  O6    . DG  E  1 4   ? 81.274  36.625  123.614 1.00 15.90 ? 4    DG  G O6    1 
ATOM   522   N  N1    . DG  E  1 4   ? 80.329  34.778  124.526 1.00 15.21 ? 4    DG  G N1    1 
ATOM   523   C  C2    . DG  E  1 4   ? 79.260  34.063  125.029 1.00 14.55 ? 4    DG  G C2    1 
ATOM   524   N  N2    . DG  E  1 4   ? 79.540  32.819  125.432 1.00 15.41 ? 4    DG  G N2    1 
ATOM   525   N  N3    . DG  E  1 4   ? 78.029  34.534  125.123 1.00 14.01 ? 4    DG  G N3    1 
ATOM   526   C  C4    . DG  E  1 4   ? 77.945  35.814  124.671 1.00 14.65 ? 4    DG  G C4    1 
ATOM   527   O  OP3   . DC  F  2 1   ? 72.249  36.871  127.858 1.00 24.19 ? 5    DC  K OP3   1 
ATOM   528   P  P     . DC  F  2 1   ? 72.352  36.378  129.304 1.00 16.79 ? 5    DC  K P     1 
ATOM   529   O  OP1   . DC  F  2 1   ? 72.882  37.419  130.276 1.00 16.41 ? 5    DC  K OP1   1 
ATOM   530   O  OP2   . DC  F  2 1   ? 71.066  35.680  129.717 1.00 16.47 ? 5    DC  K OP2   1 
ATOM   531   O  "O5'" . DC  F  2 1   ? 73.516  35.250  129.323 1.00 14.39 ? 5    DC  K "O5'" 1 
ATOM   532   C  "C5'" . DC  F  2 1   ? 73.198  33.892  129.005 1.00 16.61 ? 5    DC  K "C5'" 1 
ATOM   533   C  "C4'" . DC  F  2 1   ? 74.353  32.990  129.359 1.00 14.32 ? 5    DC  K "C4'" 1 
ATOM   534   O  "O4'" . DC  F  2 1   ? 75.399  33.192  128.360 1.00 15.75 ? 5    DC  K "O4'" 1 
ATOM   535   C  "C3'" . DC  F  2 1   ? 75.014  33.321  130.688 1.00 16.31 ? 5    DC  K "C3'" 1 
ATOM   536   O  "O3'" . DC  F  2 1   ? 74.438  32.572  131.764 1.00 13.71 ? 5    DC  K "O3'" 1 
ATOM   537   C  "C2'" . DC  F  2 1   ? 76.487  32.983  130.455 1.00 22.90 ? 5    DC  K "C2'" 1 
ATOM   538   C  "C1'" . DC  F  2 1   ? 76.682  33.056  128.945 1.00 18.56 ? 5    DC  K "C1'" 1 
ATOM   539   N  N1    . DC  F  2 1   ? 77.462  34.272  128.610 1.00 16.33 ? 5    DC  K N1    1 
ATOM   540   C  C2    . DC  F  2 1   ? 78.852  34.179  128.552 1.00 15.19 ? 5    DC  K C2    1 
ATOM   541   O  O2    . DC  F  2 1   ? 79.386  33.110  128.844 1.00 15.46 ? 5    DC  K O2    1 
ATOM   542   N  N3    . DC  F  2 1   ? 79.584  35.275  128.187 1.00 16.03 ? 5    DC  K N3    1 
ATOM   543   C  C4    . DC  F  2 1   ? 78.964  36.426  127.908 1.00 13.25 ? 5    DC  K C4    1 
ATOM   544   N  N4    . DC  F  2 1   ? 79.715  37.466  127.511 1.00 14.27 ? 5    DC  K N4    1 
ATOM   545   C  C5    . DC  F  2 1   ? 77.539  36.562  128.015 1.00 15.34 ? 5    DC  K C5    1 
ATOM   546   C  C6    . DC  F  2 1   ? 76.835  35.464  128.357 1.00 16.27 ? 5    DC  K C6    1 
ATOM   547   P  P     . DC  F  2 2   ? 74.534  33.146  133.272 1.00 14.05 ? 6    DC  K P     1 
ATOM   548   O  OP1   . DC  F  2 2   ? 73.634  32.237  134.032 1.00 15.01 ? 6    DC  K OP1   1 
ATOM   549   O  OP2   . DC  F  2 2   ? 74.335  34.596  133.391 1.00 15.57 ? 6    DC  K OP2   1 
ATOM   550   O  "O5'" . DC  F  2 2   ? 76.042  32.889  133.698 1.00 13.67 ? 6    DC  K "O5'" 1 
ATOM   551   C  "C5'" . DC  F  2 2   ? 76.562  31.551  133.651 1.00 13.21 ? 6    DC  K "C5'" 1 
ATOM   552   C  "C4'" . DC  F  2 2   ? 78.015  31.541  134.035 1.00 14.66 ? 6    DC  K "C4'" 1 
ATOM   553   O  "O4'" . DC  F  2 2   ? 78.765  32.307  133.066 1.00 14.01 ? 6    DC  K "O4'" 1 
ATOM   554   C  "C3'" . DC  F  2 2   ? 78.366  32.104  135.414 1.00 16.37 ? 6    DC  K "C3'" 1 
ATOM   555   O  "O3'" . DC  F  2 2   ? 79.190  31.085  136.014 1.00 19.28 ? 6    DC  K "O3'" 1 
ATOM   556   C  "C2'" . DC  F  2 2   ? 79.053  33.427  135.099 1.00 17.86 ? 6    DC  K "C2'" 1 
ATOM   557   C  "C1'" . DC  F  2 2   ? 79.626  33.220  133.701 1.00 15.19 ? 6    DC  K "C1'" 1 
ATOM   558   N  N1    . DC  F  2 2   ? 79.669  34.438  132.851 1.00 15.15 ? 6    DC  K N1    1 
ATOM   559   C  C2    . DC  F  2 2   ? 80.914  34.946  132.444 1.00 14.89 ? 6    DC  K C2    1 
ATOM   560   O  O2    . DC  F  2 2   ? 81.972  34.334  132.758 1.00 15.58 ? 6    DC  K O2    1 
ATOM   561   N  N3    . DC  F  2 2   ? 80.948  36.099  131.716 1.00 12.74 ? 6    DC  K N3    1 
ATOM   562   C  C4    . DC  F  2 2   ? 79.799  36.720  131.388 1.00 13.83 ? 6    DC  K C4    1 
ATOM   563   N  N4    . DC  F  2 2   ? 79.889  37.866  130.713 1.00 14.42 ? 6    DC  K N4    1 
ATOM   564   C  C5    . DC  F  2 2   ? 78.523  36.195  131.750 1.00 13.13 ? 6    DC  K C5    1 
ATOM   565   C  C6    . DC  F  2 2   ? 78.504  35.060  132.479 1.00 13.43 ? 6    DC  K C6    1 
ATOM   566   P  P     . DG  F  2 3   ? 80.321  31.416  137.105 1.00 17.58 ? 7    DG  K P     1 
ATOM   567   O  OP1   . DG  F  2 3   ? 80.649  30.074  137.655 1.00 21.73 ? 7    DG  K OP1   1 
ATOM   568   O  OP2   . DG  F  2 3   ? 80.030  32.522  138.032 1.00 18.49 ? 7    DG  K OP2   1 
ATOM   569   O  "O5'" . DG  F  2 3   ? 81.555  31.906  136.236 1.00 18.19 ? 7    DG  K "O5'" 1 
ATOM   570   C  "C5'" . DG  F  2 3   ? 82.328  30.981  135.475 1.00 18.92 ? 7    DG  K "C5'" 1 
ATOM   571   C  "C4'" . DG  F  2 3   ? 83.795  31.279  135.673 1.00 16.33 ? 7    DG  K "C4'" 1 
ATOM   572   O  "O4'" . DG  F  2 3   ? 84.086  32.600  135.141 1.00 16.08 ? 7    DG  K "O4'" 1 
ATOM   573   C  "C3'" . DG  F  2 3   ? 84.205  31.315  137.147 1.00 17.10 ? 7    DG  K "C3'" 1 
ATOM   574   O  "O3'" . DG  F  2 3   ? 85.505  30.730  137.252 1.00 18.73 ? 7    DG  K "O3'" 1 
ATOM   575   C  "C2'" . DG  F  2 3   ? 84.148  32.796  137.506 1.00 17.81 ? 7    DG  K "C2'" 1 
ATOM   576   C  "C1'" . DG  F  2 3   ? 84.402  33.525  136.181 1.00 15.66 ? 7    DG  K "C1'" 1 
ATOM   577   N  N9    . DG  F  2 3   ? 83.549  34.705  135.997 1.00 15.78 ? 7    DG  K N9    1 
ATOM   578   C  C8    . DG  F  2 3   ? 82.256  34.888  136.446 1.00 17.84 ? 7    DG  K C8    1 
ATOM   579   N  N7    . DG  F  2 3   ? 81.752  36.047  136.100 1.00 17.25 ? 7    DG  K N7    1 
ATOM   580   C  C5    . DG  F  2 3   ? 82.769  36.660  135.377 1.00 16.60 ? 7    DG  K C5    1 
ATOM   581   C  C6    . DG  F  2 3   ? 82.810  37.931  134.722 1.00 18.02 ? 7    DG  K C6    1 
ATOM   582   O  O6    . DG  F  2 3   ? 81.924  38.773  134.638 1.00 16.77 ? 7    DG  K O6    1 
ATOM   583   N  N1    . DG  F  2 3   ? 84.044  38.164  134.118 1.00 13.50 ? 7    DG  K N1    1 
ATOM   584   C  C2    . DG  F  2 3   ? 85.094  37.280  134.126 1.00 13.23 ? 7    DG  K C2    1 
ATOM   585   N  N2    . DG  F  2 3   ? 86.206  37.659  133.473 1.00 13.54 ? 7    DG  K N2    1 
ATOM   586   N  N3    . DG  F  2 3   ? 85.060  36.096  134.726 1.00 15.29 ? 7    DG  K N3    1 
ATOM   587   C  C4    . DG  F  2 3   ? 83.886  35.852  135.321 1.00 13.89 ? 7    DG  K C4    1 
ATOM   588   P  P     . DG  F  2 4   ? 86.379  30.897  138.588 1.00 19.87 ? 8    DG  K P     1 
ATOM   589   O  OP1   . DG  F  2 4   ? 87.192  29.652  138.675 1.00 23.70 ? 8    DG  K OP1   1 
ATOM   590   O  OP2   . DG  F  2 4   ? 85.578  31.349  139.737 1.00 22.13 ? 8    DG  K OP2   1 
ATOM   591   O  "O5'" . DG  F  2 4   ? 87.359  32.091  138.212 1.00 19.13 ? 8    DG  K "O5'" 1 
ATOM   592   C  "C5'" . DG  F  2 4   ? 88.131  32.032  137.012 1.00 18.48 ? 8    DG  K "C5'" 1 
ATOM   593   C  "C4'" . DG  F  2 4   ? 89.009  33.254  136.903 1.00 19.26 ? 8    DG  K "C4'" 1 
ATOM   594   O  "O4'" . DG  F  2 4   ? 88.186  34.420  136.657 1.00 18.14 ? 8    DG  K "O4'" 1 
ATOM   595   C  "C3'" . DG  F  2 4   ? 89.820  33.553  138.167 1.00 17.17 ? 8    DG  K "C3'" 1 
ATOM   596   O  "O3'" . DG  F  2 4   ? 91.148  33.872  137.753 1.00 18.56 ? 8    DG  K "O3'" 1 
ATOM   597   C  "C2'" . DG  F  2 4   ? 89.113  34.755  138.787 1.00 16.40 ? 8    DG  K "C2'" 1 
ATOM   598   C  "C1'" . DG  F  2 4   ? 88.523  35.459  137.573 1.00 17.24 ? 8    DG  K "C1'" 1 
ATOM   599   N  N9    . DG  F  2 4   ? 87.299  36.207  137.848 1.00 14.41 ? 8    DG  K N9    1 
ATOM   600   C  C8    . DG  F  2 4   ? 86.198  35.763  138.540 1.00 17.76 ? 8    DG  K C8    1 
ATOM   601   N  N7    . DG  F  2 4   ? 85.218  36.628  138.551 1.00 16.11 ? 8    DG  K N7    1 
ATOM   602   C  C5    . DG  F  2 4   ? 85.710  37.722  137.844 1.00 14.54 ? 8    DG  K C5    1 
ATOM   603   C  C6    . DG  F  2 4   ? 85.106  38.986  137.555 1.00 13.90 ? 8    DG  K C6    1 
ATOM   604   O  O6    . DG  F  2 4   ? 83.982  39.391  137.864 1.00 16.37 ? 8    DG  K O6    1 
ATOM   605   N  N1    . DG  F  2 4   ? 85.964  39.813  136.839 1.00 14.39 ? 8    DG  K N1    1 
ATOM   606   C  C2    . DG  F  2 4   ? 87.225  39.476  136.440 1.00 14.60 ? 8    DG  K C2    1 
ATOM   607   N  N2    . DG  F  2 4   ? 87.870  40.410  135.718 1.00 14.47 ? 8    DG  K N2    1 
ATOM   608   N  N3    . DG  F  2 4   ? 87.807  38.312  136.715 1.00 14.74 ? 8    DG  K N3    1 
ATOM   609   C  C4    . DG  F  2 4   ? 86.997  37.489  137.418 1.00 15.36 ? 8    DG  K C4    1 
ATOM   610   P  P     . DC  F  2 5   ? 92.319  34.031  138.836 1.00 21.69 ? 9    DC  K P     1 
ATOM   611   O  OP1   . DC  F  2 5   ? 93.578  33.756  138.091 1.00 25.81 ? 9    DC  K OP1   1 
ATOM   612   O  OP2   . DC  F  2 5   ? 92.016  33.293  140.091 1.00 21.86 ? 9    DC  K OP2   1 
ATOM   613   O  "O5'" . DC  F  2 5   ? 92.271  35.568  139.208 1.00 18.64 ? 9    DC  K "O5'" 1 
ATOM   614   C  "C5'" . DC  F  2 5   ? 92.577  36.548  138.217 1.00 18.12 ? 9    DC  K "C5'" 1 
ATOM   615   C  "C4'" . DC  F  2 5   ? 92.420  37.928  138.800 1.00 17.85 ? 9    DC  K "C4'" 1 
ATOM   616   O  "O4'" . DC  F  2 5   ? 91.014  38.236  138.944 1.00 17.58 ? 9    DC  K "O4'" 1 
ATOM   617   C  "C3'" . DC  F  2 5   ? 93.035  38.080  140.194 1.00 19.08 ? 9    DC  K "C3'" 1 
ATOM   618   O  "O3'" . DC  F  2 5   ? 93.764  39.297  140.242 1.00 20.40 ? 9    DC  K "O3'" 1 
ATOM   619   C  "C2'" . DC  F  2 5   ? 91.825  38.172  141.113 1.00 17.93 ? 9    DC  K "C2'" 1 
ATOM   620   C  "C1'" . DC  F  2 5   ? 90.810  38.856  140.208 1.00 14.84 ? 9    DC  K "C1'" 1 
ATOM   621   N  N1    . DC  F  2 5   ? 89.387  38.681  140.560 1.00 18.50 ? 9    DC  K N1    1 
ATOM   622   C  C2    . DC  F  2 5   ? 88.493  39.732  140.277 1.00 17.29 ? 9    DC  K C2    1 
ATOM   623   O  O2    . DC  F  2 5   ? 88.939  40.774  139.780 1.00 17.45 ? 9    DC  K O2    1 
ATOM   624   N  N3    . DC  F  2 5   ? 87.179  39.583  140.544 1.00 13.83 ? 9    DC  K N3    1 
ATOM   625   C  C4    . DC  F  2 5   ? 86.735  38.436  141.077 1.00 15.36 ? 9    DC  K C4    1 
ATOM   626   N  N4    . DC  F  2 5   ? 85.431  38.346  141.337 1.00 18.75 ? 9    DC  K N4    1 
ATOM   627   C  C5    . DC  F  2 5   ? 87.617  37.349  141.373 1.00 15.30 ? 9    DC  K C5    1 
ATOM   628   C  C6    . DC  F  2 5   ? 88.919  37.516  141.119 1.00 18.99 ? 9    DC  K C6    1 
ATOM   629   P  P     . DG  F  2 6   ? 95.347  39.283  139.986 1.00 22.07 ? 10   DG  K P     1 
ATOM   630   O  OP1   . DG  F  2 6   ? 95.652  38.366  138.867 1.00 19.70 ? 10   DG  K OP1   1 
ATOM   631   O  OP2   . DG  F  2 6   ? 96.031  39.091  141.308 1.00 25.04 ? 10   DG  K OP2   1 
ATOM   632   O  "O5'" . DG  F  2 6   ? 95.631  40.795  139.565 1.00 20.45 ? 10   DG  K "O5'" 1 
ATOM   633   C  "C5'" . DG  F  2 6   ? 95.307  41.255  138.242 1.00 22.81 ? 10   DG  K "C5'" 1 
ATOM   634   C  "C4'" . DG  F  2 6   ? 94.787  42.673  138.281 1.00 17.76 ? 10   DG  K "C4'" 1 
ATOM   635   O  "O4'" . DG  F  2 6   ? 93.541  42.767  138.992 1.00 22.57 ? 10   DG  K "O4'" 1 
ATOM   636   C  "C3'" . DG  F  2 6   ? 95.693  43.725  138.912 1.00 23.34 ? 10   DG  K "C3'" 1 
ATOM   637   O  "O3'" . DG  F  2 6   ? 95.390  44.945  138.242 1.00 20.90 ? 10   DG  K "O3'" 1 
ATOM   638   C  "C2'" . DG  F  2 6   ? 95.202  43.774  140.345 1.00 26.61 ? 10   DG  K "C2'" 1 
ATOM   639   C  "C1'" . DG  F  2 6   ? 93.718  43.516  140.198 1.00 24.79 ? 10   DG  K "C1'" 1 
ATOM   640   N  N9    . DG  F  2 6   ? 93.176  42.681  141.255 1.00 25.05 ? 10   DG  K N9    1 
ATOM   641   C  C8    . DG  F  2 6   ? 93.800  41.668  141.954 1.00 26.33 ? 10   DG  K C8    1 
ATOM   642   N  N7    . DG  F  2 6   ? 92.987  41.024  142.745 1.00 28.59 ? 10   DG  K N7    1 
ATOM   643   C  C5    . DG  F  2 6   ? 91.774  41.675  142.569 1.00 20.71 ? 10   DG  K C5    1 
ATOM   644   C  C6    . DG  F  2 6   ? 90.511  41.412  143.115 1.00 27.37 ? 10   DG  K C6    1 
ATOM   645   O  O6    . DG  F  2 6   ? 90.174  40.487  143.866 1.00 33.87 ? 10   DG  K O6    1 
ATOM   646   N  N1    . DG  F  2 6   ? 89.567  42.344  142.686 1.00 22.84 ? 10   DG  K N1    1 
ATOM   647   C  C2    . DG  F  2 6   ? 89.813  43.371  141.817 1.00 27.17 ? 10   DG  K C2    1 
ATOM   648   N  N2    . DG  F  2 6   ? 88.804  44.187  141.556 1.00 24.62 ? 10   DG  K N2    1 
ATOM   649   N  N3    . DG  F  2 6   ? 90.976  43.591  141.257 1.00 21.49 ? 10   DG  K N3    1 
ATOM   650   C  C4    . DG  F  2 6   ? 91.904  42.720  141.680 1.00 21.12 ? 10   DG  K C4    1 
ATOM   651   P  P     . DC  F  2 7   ? 96.076  46.332  138.684 1.00 21.66 ? 11   DC  K P     1 
ATOM   652   O  OP1   . DC  F  2 7   ? 96.497  46.926  137.371 1.00 22.91 ? 11   DC  K OP1   1 
ATOM   653   O  OP2   . DC  F  2 7   ? 97.106  46.119  139.750 1.00 26.83 ? 11   DC  K OP2   1 
ATOM   654   O  "O5'" . DC  F  2 7   ? 94.864  47.170  139.257 1.00 22.08 ? 11   DC  K "O5'" 1 
ATOM   655   C  "C5'" . DC  F  2 7   ? 93.788  47.542  138.398 1.00 22.42 ? 11   DC  K "C5'" 1 
ATOM   656   C  "C4'" . DC  F  2 7   ? 92.628  48.064  139.210 1.00 24.69 ? 11   DC  K "C4'" 1 
ATOM   657   O  "O4'" . DC  F  2 7   ? 92.172  47.023  140.103 1.00 25.82 ? 11   DC  K "O4'" 1 
ATOM   658   C  "C3'" . DC  F  2 7   ? 92.994  49.255  140.093 1.00 26.86 ? 11   DC  K "C3'" 1 
ATOM   659   O  "O3'" . DC  F  2 7   ? 92.744  50.517  139.542 1.00 24.80 ? 11   DC  K "O3'" 1 
ATOM   660   C  "C2'" . DC  F  2 7   ? 92.418  48.946  141.464 1.00 28.38 ? 11   DC  K "C2'" 1 
ATOM   661   C  "C1'" . DC  F  2 7   ? 91.716  47.600  141.333 1.00 28.86 ? 11   DC  K "C1'" 1 
ATOM   662   N  N1    . DC  F  2 7   ? 92.142  46.674  142.401 1.00 21.78 ? 11   DC  K N1    1 
ATOM   663   C  C2    . DC  F  2 7   ? 91.203  46.224  143.336 1.00 21.25 ? 11   DC  K C2    1 
ATOM   664   O  O2    . DC  F  2 7   ? 90.052  46.692  143.311 1.00 25.36 ? 11   DC  K O2    1 
ATOM   665   N  N3    . DC  F  2 7   ? 91.582  45.288  144.242 1.00 25.06 ? 11   DC  K N3    1 
ATOM   666   C  C4    . DC  F  2 7   ? 92.832  44.821  144.240 1.00 20.72 ? 11   DC  K C4    1 
ATOM   667   N  N4    . DC  F  2 7   ? 93.150  43.841  145.111 1.00 25.93 ? 11   DC  K N4    1 
ATOM   668   C  C5    . DC  F  2 7   ? 93.817  45.313  143.341 1.00 23.04 ? 11   DC  K C5    1 
ATOM   669   C  C6    . DC  F  2 7   ? 93.433  46.234  142.445 1.00 23.84 ? 11   DC  K C6    1 
ATOM   670   O  "O5'" . DT  G  1 1   ? 91.278  41.240  150.247 1.00 44.70 ? 1    DT  H "O5'" 1 
ATOM   671   C  "C5'" . DT  G  1 1   ? 90.931  40.740  151.542 1.00 44.92 ? 1    DT  H "C5'" 1 
ATOM   672   C  "C4'" . DT  G  1 1   ? 89.584  41.234  152.027 1.00 41.53 ? 1    DT  H "C4'" 1 
ATOM   673   O  "O4'" . DT  G  1 1   ? 89.554  42.685  151.972 1.00 39.70 ? 1    DT  H "O4'" 1 
ATOM   674   C  "C3'" . DT  G  1 1   ? 88.391  40.755  151.197 1.00 40.43 ? 1    DT  H "C3'" 1 
ATOM   675   O  "O3'" . DT  G  1 1   ? 87.261  40.530  152.054 1.00 35.23 ? 1    DT  H "O3'" 1 
ATOM   676   C  "C2'" . DT  G  1 1   ? 88.120  41.936  150.282 1.00 38.01 ? 1    DT  H "C2'" 1 
ATOM   677   C  "C1'" . DT  G  1 1   ? 88.456  43.115  151.176 1.00 39.77 ? 1    DT  H "C1'" 1 
ATOM   678   N  N1    . DT  G  1 1   ? 88.865  44.333  150.446 1.00 36.98 ? 1    DT  H N1    1 
ATOM   679   C  C2    . DT  G  1 1   ? 88.056  45.449  150.528 1.00 39.91 ? 1    DT  H C2    1 
ATOM   680   O  O2    . DT  G  1 1   ? 87.017  45.488  151.182 1.00 38.09 ? 1    DT  H O2    1 
ATOM   681   N  N3    . DT  G  1 1   ? 88.504  46.529  149.810 1.00 38.84 ? 1    DT  H N3    1 
ATOM   682   C  C4    . DT  G  1 1   ? 89.646  46.607  149.039 1.00 38.94 ? 1    DT  H C4    1 
ATOM   683   O  O4    . DT  G  1 1   ? 89.902  47.643  148.440 1.00 43.34 ? 1    DT  H O4    1 
ATOM   684   C  C5    . DT  G  1 1   ? 90.451  45.409  149.008 1.00 39.65 ? 1    DT  H C5    1 
ATOM   685   C  C7    . DT  G  1 1   ? 91.719  45.406  148.206 1.00 39.31 ? 1    DT  H C7    1 
ATOM   686   C  C6    . DT  G  1 1   ? 90.028  44.345  149.702 1.00 36.54 ? 1    DT  H C6    1 
ATOM   687   P  P     . DG  G  1 2   ? 86.123  39.478  151.623 1.00 38.44 ? 2    DG  H P     1 
ATOM   688   O  OP1   . DG  G  1 2   ? 85.313  39.132  152.827 1.00 42.19 ? 2    DG  H OP1   1 
ATOM   689   O  OP2   . DG  G  1 2   ? 86.763  38.393  150.824 1.00 34.09 ? 2    DG  H OP2   1 
ATOM   690   O  "O5'" . DG  G  1 2   ? 85.163  40.280  150.629 1.00 39.60 ? 2    DG  H "O5'" 1 
ATOM   691   C  "C5'" . DG  G  1 2   ? 84.372  41.375  151.095 1.00 39.63 ? 2    DG  H "C5'" 1 
ATOM   692   C  "C4'" . DG  G  1 2   ? 83.909  42.229  149.935 1.00 39.41 ? 2    DG  H "C4'" 1 
ATOM   693   O  "O4'" . DG  G  1 2   ? 85.041  42.718  149.174 1.00 38.47 ? 2    DG  H "O4'" 1 
ATOM   694   C  "C3'" . DG  G  1 2   ? 82.992  41.569  148.908 1.00 44.08 ? 2    DG  H "C3'" 1 
ATOM   695   O  "O3'" . DG  G  1 2   ? 82.099  42.596  148.462 1.00 48.97 ? 2    DG  H "O3'" 1 
ATOM   696   C  "C2'" . DG  G  1 2   ? 83.960  41.128  147.817 1.00 39.26 ? 2    DG  H "C2'" 1 
ATOM   697   C  "C1'" . DG  G  1 2   ? 84.986  42.252  147.824 1.00 34.14 ? 2    DG  H "C1'" 1 
ATOM   698   N  N9    . DG  G  1 2   ? 86.355  41.896  147.444 1.00 28.29 ? 2    DG  H N9    1 
ATOM   699   C  C8    . DG  G  1 2   ? 87.038  40.734  147.719 1.00 27.32 ? 2    DG  H C8    1 
ATOM   700   N  N7    . DG  G  1 2   ? 88.304  40.794  147.391 1.00 29.20 ? 2    DG  H N7    1 
ATOM   701   C  C5    . DG  G  1 2   ? 88.448  42.055  146.827 1.00 25.72 ? 2    DG  H C5    1 
ATOM   702   C  C6    . DG  G  1 2   ? 89.601  42.711  146.300 1.00 30.03 ? 2    DG  H C6    1 
ATOM   703   O  O6    . DG  G  1 2   ? 90.774  42.321  146.269 1.00 29.75 ? 2    DG  H O6    1 
ATOM   704   N  N1    . DG  G  1 2   ? 89.284  43.960  145.792 1.00 27.35 ? 2    DG  H N1    1 
ATOM   705   C  C2    . DG  G  1 2   ? 88.041  44.522  145.804 1.00 27.53 ? 2    DG  H C2    1 
ATOM   706   N  N2    . DG  G  1 2   ? 87.945  45.728  145.265 1.00 28.85 ? 2    DG  H N2    1 
ATOM   707   N  N3    . DG  G  1 2   ? 86.969  43.943  146.312 1.00 29.11 ? 2    DG  H N3    1 
ATOM   708   C  C4    . DG  G  1 2   ? 87.245  42.723  146.806 1.00 28.93 ? 2    DG  H C4    1 
ATOM   709   P  P     . DC  G  1 3   ? 81.006  42.298  147.327 1.00 59.85 ? 3    DC  H P     1 
ATOM   710   O  OP1   . DC  G  1 3   ? 79.653  42.434  147.913 1.00 58.25 ? 3    DC  H OP1   1 
ATOM   711   O  OP2   . DC  G  1 3   ? 81.370  41.067  146.567 1.00 55.89 ? 3    DC  H OP2   1 
ATOM   712   O  "O5'" . DC  G  1 3   ? 81.187  43.537  146.353 1.00 56.55 ? 3    DC  H "O5'" 1 
ATOM   713   C  "C5'" . DC  G  1 3   ? 82.052  44.608  146.712 1.00 50.81 ? 3    DC  H "C5'" 1 
ATOM   714   C  "C4'" . DC  G  1 3   ? 82.667  45.182  145.462 1.00 47.16 ? 3    DC  H "C4'" 1 
ATOM   715   O  "O4'" . DC  G  1 3   ? 83.913  44.529  145.114 1.00 45.57 ? 3    DC  H "O4'" 1 
ATOM   716   C  "C3'" . DC  G  1 3   ? 81.749  45.005  144.263 1.00 42.73 ? 3    DC  H "C3'" 1 
ATOM   717   O  "O3'" . DC  G  1 3   ? 81.877  46.173  143.507 1.00 45.02 ? 3    DC  H "O3'" 1 
ATOM   718   C  "C2'" . DC  G  1 3   ? 82.356  43.823  143.519 1.00 41.63 ? 3    DC  H "C2'" 1 
ATOM   719   C  "C1'" . DC  G  1 3   ? 83.838  44.008  143.793 1.00 39.12 ? 3    DC  H "C1'" 1 
ATOM   720   N  N1    . DC  G  1 3   ? 84.681  42.797  143.771 1.00 34.88 ? 3    DC  H N1    1 
ATOM   721   C  C2    . DC  G  1 3   ? 85.994  42.932  143.367 1.00 30.47 ? 3    DC  H C2    1 
ATOM   722   O  O2    . DC  G  1 3   ? 86.362  44.020  142.921 1.00 32.11 ? 3    DC  H O2    1 
ATOM   723   N  N3    . DC  G  1 3   ? 86.835  41.877  143.465 1.00 29.89 ? 3    DC  H N3    1 
ATOM   724   C  C4    . DC  G  1 3   ? 86.387  40.714  143.926 1.00 29.90 ? 3    DC  H C4    1 
ATOM   725   N  N4    . DC  G  1 3   ? 87.273  39.715  144.074 1.00 29.97 ? 3    DC  H N4    1 
ATOM   726   C  C5    . DC  G  1 3   ? 85.018  40.525  144.277 1.00 31.54 ? 3    DC  H C5    1 
ATOM   727   C  C6    . DC  G  1 3   ? 84.205  41.588  144.183 1.00 30.81 ? 3    DC  H C6    1 
ATOM   728   P  P     . DG  G  1 4   ? 80.584  46.975  143.042 1.00 40.05 ? 4    DG  H P     1 
ATOM   729   O  OP1   . DG  G  1 4   ? 80.354  48.145  143.910 1.00 36.39 ? 4    DG  H OP1   1 
ATOM   730   O  OP2   . DG  G  1 4   ? 79.450  46.040  142.749 1.00 40.64 ? 4    DG  H OP2   1 
ATOM   731   O  "O5'" . DG  G  1 4   ? 81.152  47.604  141.700 1.00 35.32 ? 4    DG  H "O5'" 1 
ATOM   732   C  "C5'" . DG  G  1 4   ? 82.338  48.400  141.770 1.00 31.02 ? 4    DG  H "C5'" 1 
ATOM   733   C  "C4'" . DG  G  1 4   ? 83.163  48.233  140.519 1.00 26.70 ? 4    DG  H "C4'" 1 
ATOM   734   O  "O4'" . DG  G  1 4   ? 83.690  46.887  140.423 1.00 27.79 ? 4    DG  H "O4'" 1 
ATOM   735   C  "C3'" . DG  G  1 4   ? 82.372  48.463  139.238 1.00 28.02 ? 4    DG  H "C3'" 1 
ATOM   736   O  "O3'" . DG  G  1 4   ? 83.334  48.978  138.319 1.00 25.93 ? 4    DG  H "O3'" 1 
ATOM   737   C  "C2'" . DG  G  1 4   ? 81.975  47.056  138.840 1.00 23.57 ? 4    DG  H "C2'" 1 
ATOM   738   C  "C1'" . DG  G  1 4   ? 83.202  46.264  139.229 1.00 23.51 ? 4    DG  H "C1'" 1 
ATOM   739   N  N9    . DG  G  1 4   ? 82.979  44.866  139.562 1.00 16.04 ? 4    DG  H N9    1 
ATOM   740   C  C8    . DG  G  1 4   ? 81.812  44.270  139.977 1.00 15.86 ? 4    DG  H C8    1 
ATOM   741   N  N7    . DG  G  1 4   ? 81.978  43.032  140.344 1.00 16.46 ? 4    DG  H N7    1 
ATOM   742   C  C5    . DG  G  1 4   ? 83.331  42.794  140.129 1.00 17.69 ? 4    DG  H C5    1 
ATOM   743   C  C6    . DG  G  1 4   ? 84.105  41.638  140.377 1.00 16.13 ? 4    DG  H C6    1 
ATOM   744   O  O6    . DG  G  1 4   ? 83.751  40.574  140.901 1.00 17.88 ? 4    DG  H O6    1 
ATOM   745   N  N1    . DG  G  1 4   ? 85.429  41.812  139.979 1.00 15.85 ? 4    DG  H N1    1 
ATOM   746   C  C2    . DG  G  1 4   ? 85.946  42.959  139.438 1.00 13.70 ? 4    DG  H C2    1 
ATOM   747   N  N2    . DG  G  1 4   ? 87.251  42.922  139.085 1.00 13.97 ? 4    DG  H N2    1 
ATOM   748   N  N3    . DG  G  1 4   ? 85.242  44.064  139.242 1.00 15.40 ? 4    DG  H N3    1 
ATOM   749   C  C4    . DG  G  1 4   ? 83.950  43.901  139.604 1.00 17.62 ? 4    DG  H C4    1 
ATOM   750   O  OP3   . DC  H  2 1   ? 81.976  49.274  136.180 1.00 21.71 ? 5    DC  L OP3   1 
ATOM   751   P  P     . DC  H  2 1   ? 82.528  49.251  134.759 1.00 17.38 ? 5    DC  L P     1 
ATOM   752   O  OP1   . DC  H  2 1   ? 81.664  48.479  133.800 1.00 14.67 ? 5    DC  L OP1   1 
ATOM   753   O  OP2   . DC  H  2 1   ? 82.930  50.635  134.294 1.00 16.59 ? 5    DC  L OP2   1 
ATOM   754   O  "O5'" . DC  H  2 1   ? 83.884  48.360  134.836 1.00 15.29 ? 5    DC  L "O5'" 1 
ATOM   755   C  "C5'" . DC  H  2 1   ? 85.128  48.970  135.150 1.00 15.30 ? 5    DC  L "C5'" 1 
ATOM   756   C  "C4'" . DC  H  2 1   ? 86.252  47.990  134.936 1.00 14.34 ? 5    DC  L "C4'" 1 
ATOM   757   O  "O4'" . DC  H  2 1   ? 86.169  46.996  135.997 1.00 16.15 ? 5    DC  L "O4'" 1 
ATOM   758   C  "C3'" . DC  H  2 1   ? 86.115  47.185  133.647 1.00 14.49 ? 5    DC  L "C3'" 1 
ATOM   759   O  "O3'" . DC  H  2 1   ? 86.782  47.834  132.581 1.00 12.88 ? 5    DC  L "O3'" 1 
ATOM   760   C  "C2'" . DC  H  2 1   ? 86.790  45.869  133.994 1.00 19.29 ? 5    DC  L "C2'" 1 
ATOM   761   C  "C1'" . DC  H  2 1   ? 86.630  45.732  135.506 1.00 16.05 ? 5    DC  L "C1'" 1 
ATOM   762   N  N1    . DC  H  2 1   ? 85.561  44.745  135.763 1.00 13.07 ? 5    DC  L N1    1 
ATOM   763   C  C2    . DC  H  2 1   ? 85.926  43.382  135.909 1.00 12.40 ? 5    DC  L C2    1 
ATOM   764   O  O2    . DC  H  2 1   ? 87.105  43.063  135.706 1.00 14.04 ? 5    DC  L O2    1 
ATOM   765   N  N3    . DC  H  2 1   ? 84.969  42.477  136.242 1.00 12.30 ? 5    DC  L N3    1 
ATOM   766   C  C4    . DC  H  2 1   ? 83.698  42.864  136.391 1.00 12.19 ? 5    DC  L C4    1 
ATOM   767   N  N4    . DC  H  2 1   ? 82.800  41.944  136.787 1.00 14.13 ? 5    DC  L N4    1 
ATOM   768   C  C5    . DC  H  2 1   ? 83.283  44.226  136.161 1.00 12.79 ? 5    DC  L C5    1 
ATOM   769   C  C6    . DC  H  2 1   ? 84.244  45.123  135.867 1.00 13.00 ? 5    DC  L C6    1 
ATOM   770   P  P     . DC  H  2 2   ? 86.314  47.546  131.048 1.00 12.99 ? 6    DC  L P     1 
ATOM   771   O  OP1   . DC  H  2 2   ? 87.060  48.561  130.272 1.00 13.78 ? 6    DC  L OP1   1 
ATOM   772   O  OP2   . DC  H  2 2   ? 84.859  47.460  130.945 1.00 13.82 ? 6    DC  L OP2   1 
ATOM   773   O  "O5'" . DC  H  2 2   ? 86.940  46.122  130.726 1.00 14.17 ? 6    DC  L "O5'" 1 
ATOM   774   C  "C5'" . DC  H  2 2   ? 88.343  45.905  130.897 1.00 13.28 ? 6    DC  L "C5'" 1 
ATOM   775   C  "C4'" . DC  H  2 2   ? 88.691  44.469  130.608 1.00 14.24 ? 6    DC  L "C4'" 1 
ATOM   776   O  "O4'" . DC  H  2 2   ? 88.053  43.615  131.596 1.00 12.95 ? 6    DC  L "O4'" 1 
ATOM   777   C  "C3'" . DC  H  2 2   ? 88.312  43.905  129.232 1.00 15.06 ? 6    DC  L "C3'" 1 
ATOM   778   O  "O3'" . DC  H  2 2   ? 89.511  43.246  128.794 1.00 14.64 ? 6    DC  L "O3'" 1 
ATOM   779   C  "C2'" . DC  H  2 2   ? 87.116  43.008  129.532 1.00 14.69 ? 6    DC  L "C2'" 1 
ATOM   780   C  "C1'" . DC  H  2 2   ? 87.368  42.548  130.968 1.00 14.18 ? 6    DC  L "C1'" 1 
ATOM   781   N  N1    . DC  H  2 2   ? 86.136  42.310  131.738 1.00 14.18 ? 6    DC  L N1    1 
ATOM   782   C  C2    . DC  H  2 2   ? 85.855  41.016  132.224 1.00 15.42 ? 6    DC  L C2    1 
ATOM   783   O  O2    . DC  H  2 2   ? 86.706  40.104  132.061 1.00 13.55 ? 6    DC  L O2    1 
ATOM   784   N  N3    . DC  H  2 2   ? 84.670  40.799  132.873 1.00 12.84 ? 6    DC  L N3    1 
ATOM   785   C  C4    . DC  H  2 2   ? 83.804  41.802  133.048 1.00 11.53 ? 6    DC  L C4    1 
ATOM   786   N  N4    . DC  H  2 2   ? 82.611  41.530  133.605 1.00 13.97 ? 6    DC  L N4    1 
ATOM   787   C  C5    . DC  H  2 2   ? 84.104  43.138  132.627 1.00 13.08 ? 6    DC  L C5    1 
ATOM   788   C  C6    . DC  H  2 2   ? 85.259  43.342  131.978 1.00 12.33 ? 6    DC  L C6    1 
ATOM   789   P  P     . DG  H  2 3   ? 89.527  42.026  127.749 1.00 16.23 ? 7    DG  L P     1 
ATOM   790   O  OP1   . DG  H  2 3   ? 90.968  41.998  127.353 1.00 18.24 ? 7    DG  L OP1   1 
ATOM   791   O  OP2   . DG  H  2 3   ? 88.462  42.034  126.723 1.00 16.57 ? 7    DG  L OP2   1 
ATOM   792   O  "O5'" . DG  H  2 3   ? 89.233  40.764  128.664 1.00 15.23 ? 7    DG  L "O5'" 1 
ATOM   793   C  "C5'" . DG  H  2 3   ? 90.233  40.266  129.544 1.00 16.36 ? 7    DG  L "C5'" 1 
ATOM   794   C  "C4'" . DG  H  2 3   ? 90.260  38.762  129.473 1.00 16.04 ? 7    DG  L "C4'" 1 
ATOM   795   O  "O4'" . DG  H  2 3   ? 88.987  38.246  129.941 1.00 15.56 ? 7    DG  L "O4'" 1 
ATOM   796   C  "C3'" . DG  H  2 3   ? 90.453  38.206  128.065 1.00 16.73 ? 7    DG  L "C3'" 1 
ATOM   797   O  "O3'" . DG  H  2 3   ? 91.288  37.046  128.176 1.00 17.18 ? 7    DG  L "O3'" 1 
ATOM   798   C  "C2'" . DG  H  2 3   ? 89.031  37.912  127.604 1.00 17.68 ? 7    DG  L "C2'" 1 
ATOM   799   C  "C1'" . DG  H  2 3   ? 88.245  37.649  128.887 1.00 15.47 ? 7    DG  L "C1'" 1 
ATOM   800   N  N9    . DG  H  2 3   ? 86.904  38.245  128.906 1.00 13.06 ? 7    DG  L N9    1 
ATOM   801   C  C8    . DG  H  2 3   ? 86.498  39.436  128.326 1.00 14.88 ? 7    DG  L C8    1 
ATOM   802   N  N7    . DG  H  2 3   ? 85.234  39.709  128.547 1.00 13.57 ? 7    DG  L N7    1 
ATOM   803   C  C5    . DG  H  2 3   ? 84.781  38.639  129.315 1.00 15.10 ? 7    DG  L C5    1 
ATOM   804   C  C6    . DG  H  2 3   ? 83.491  38.371  129.870 1.00 15.76 ? 7    DG  L C6    1 
ATOM   805   O  O6    . DG  H  2 3   ? 82.467  39.067  129.805 1.00 14.21 ? 7    DG  L O6    1 
ATOM   806   N  N1    . DG  H  2 3   ? 83.470  37.161  130.565 1.00 14.16 ? 7    DG  L N1    1 
ATOM   807   C  C2    . DG  H  2 3   ? 84.559  36.319  130.720 1.00 13.31 ? 7    DG  L C2    1 
ATOM   808   N  N2    . DG  H  2 3   ? 84.366  35.187  131.435 1.00 15.38 ? 7    DG  L N2    1 
ATOM   809   N  N3    . DG  H  2 3   ? 85.752  36.565  130.219 1.00 13.48 ? 7    DG  L N3    1 
ATOM   810   C  C4    . DG  H  2 3   ? 85.794  37.727  129.534 1.00 13.33 ? 7    DG  L C4    1 
ATOM   811   P  P     . DG  H  2 4   ? 91.553  36.119  126.897 1.00 18.09 ? 8    DG  L P     1 
ATOM   812   O  OP1   . DG  H  2 4   ? 92.926  35.602  127.104 1.00 21.12 ? 8    DG  L OP1   1 
ATOM   813   O  OP2   . DG  H  2 4   ? 91.216  36.835  125.661 1.00 21.35 ? 8    DG  L OP2   1 
ATOM   814   O  "O5'" . DG  H  2 4   ? 90.510  34.947  127.119 1.00 16.94 ? 8    DG  L "O5'" 1 
ATOM   815   C  "C5'" . DG  H  2 4   ? 90.538  34.239  128.360 1.00 16.88 ? 8    DG  L "C5'" 1 
ATOM   816   C  "C4'" . DG  H  2 4   ? 89.444  33.203  128.399 1.00 15.63 ? 8    DG  L "C4'" 1 
ATOM   817   O  "O4'" . DG  H  2 4   ? 88.156  33.863  128.505 1.00 17.43 ? 8    DG  L "O4'" 1 
ATOM   818   C  "C3'" . DG  H  2 4   ? 89.372  32.280  127.178 1.00 14.80 ? 8    DG  L "C3'" 1 
ATOM   819   O  "O3'" . DG  H  2 4   ? 89.257  30.941  127.676 1.00 20.71 ? 8    DG  L "O3'" 1 
ATOM   820   C  "C2'" . DG  H  2 4   ? 88.103  32.730  126.462 1.00 18.24 ? 8    DG  L "C2'" 1 
ATOM   821   C  "C1'" . DG  H  2 4   ? 87.238  33.254  127.605 1.00 16.38 ? 8    DG  L "C1'" 1 
ATOM   822   N  N9    . DG  H  2 4   ? 86.270  34.278  127.221 1.00 15.64 ? 8    DG  L N9    1 
ATOM   823   C  C8    . DG  H  2 4   ? 86.523  35.408  126.478 1.00 15.16 ? 8    DG  L C8    1 
ATOM   824   N  N7    . DG  H  2 4   ? 85.467  36.157  126.313 1.00 13.63 ? 8    DG  L N7    1 
ATOM   825   C  C5    . DG  H  2 4   ? 84.456  35.481  126.975 1.00 13.38 ? 8    DG  L C5    1 
ATOM   826   C  C6    . DG  H  2 4   ? 83.079  35.813  127.124 1.00 14.26 ? 8    DG  L C6    1 
ATOM   827   O  O6    . DG  H  2 4   ? 82.472  36.808  126.683 1.00 14.51 ? 8    DG  L O6    1 
ATOM   828   N  N1    . DG  H  2 4   ? 82.398  34.853  127.879 1.00 14.10 ? 8    DG  L N1    1 
ATOM   829   C  C2    . DG  H  2 4   ? 82.970  33.722  128.420 1.00 14.20 ? 8    DG  L C2    1 
ATOM   830   N  N2    . DG  H  2 4   ? 82.158  32.930  129.152 1.00 17.11 ? 8    DG  L N2    1 
ATOM   831   N  N3    . DG  H  2 4   ? 84.250  33.391  128.268 1.00 16.35 ? 8    DG  L N3    1 
ATOM   832   C  C4    . DG  H  2 4   ? 84.931  34.319  127.544 1.00 14.69 ? 8    DG  L C4    1 
ATOM   833   P  P     . DC  H  2 5   ? 89.391  29.684  126.688 1.00 22.24 ? 9    DC  L P     1 
ATOM   834   O  OP1   . DC  H  2 5   ? 89.834  28.553  127.544 1.00 25.81 ? 9    DC  L OP1   1 
ATOM   835   O  OP2   . DC  H  2 5   ? 90.142  30.026  125.461 1.00 22.81 ? 9    DC  L OP2   1 
ATOM   836   O  "O5'" . DC  H  2 5   ? 87.903  29.438  126.193 1.00 23.16 ? 9    DC  L "O5'" 1 
ATOM   837   C  "C5'" . DC  H  2 5   ? 86.904  28.956  127.077 1.00 25.02 ? 9    DC  L "C5'" 1 
ATOM   838   C  "C4'" . DC  H  2 5   ? 85.589  28.868  126.342 1.00 22.32 ? 9    DC  L "C4'" 1 
ATOM   839   O  "O4'" . DC  H  2 5   ? 85.054  30.204  126.141 1.00 19.81 ? 9    DC  L "O4'" 1 
ATOM   840   C  "C3'" . DC  H  2 5   ? 85.667  28.224  124.951 1.00 21.13 ? 9    DC  L "C3'" 1 
ATOM   841   O  "O3'" . DC  H  2 5   ? 84.600  27.290  124.785 1.00 26.49 ? 9    DC  L "O3'" 1 
ATOM   842   C  "C2'" . DC  H  2 5   ? 85.383  29.377  124.008 1.00 19.19 ? 9    DC  L "C2'" 1 
ATOM   843   C  "C1'" . DC  H  2 5   ? 84.464  30.238  124.867 1.00 20.29 ? 9    DC  L "C1'" 1 
ATOM   844   N  N1    . DC  H  2 5   ? 84.342  31.652  124.470 1.00 17.54 ? 9    DC  L N1    1 
ATOM   845   C  C2    . DC  H  2 5   ? 83.103  32.278  124.620 1.00 17.72 ? 9    DC  L C2    1 
ATOM   846   O  O2    . DC  H  2 5   ? 82.154  31.623  125.075 1.00 17.05 ? 9    DC  L O2    1 
ATOM   847   N  N3    . DC  H  2 5   ? 82.965  33.573  124.260 1.00 16.12 ? 9    DC  L N3    1 
ATOM   848   C  C4    . DC  H  2 5   ? 84.006  34.235  123.744 1.00 14.92 ? 9    DC  L C4    1 
ATOM   849   N  N4    . DC  H  2 5   ? 83.802  35.495  123.364 1.00 16.47 ? 9    DC  L N4    1 
ATOM   850   C  C5    . DC  H  2 5   ? 85.288  33.627  123.588 1.00 17.54 ? 9    DC  L C5    1 
ATOM   851   C  C6    . DC  H  2 5   ? 85.411  32.342  123.967 1.00 17.21 ? 9    DC  L C6    1 
ATOM   852   P  P     . DG  H  2 6   ? 84.841  25.739  125.100 1.00 26.28 ? 10   DG  L P     1 
ATOM   853   O  OP1   . DG  H  2 6   ? 85.677  25.616  126.301 1.00 26.30 ? 10   DG  L OP1   1 
ATOM   854   O  OP2   . DG  H  2 6   ? 85.246  25.079  123.832 1.00 29.80 ? 10   DG  L OP2   1 
ATOM   855   O  "O5'" . DG  H  2 6   ? 83.361  25.241  125.443 1.00 24.77 ? 10   DG  L "O5'" 1 
ATOM   856   C  "C5'" . DG  H  2 6   ? 82.775  25.542  126.710 1.00 24.30 ? 10   DG  L "C5'" 1 
ATOM   857   C  "C4'" . DG  H  2 6   ? 81.298  25.810  126.549 1.00 23.81 ? 10   DG  L "C4'" 1 
ATOM   858   O  "O4'" . DG  H  2 6   ? 81.053  27.069  125.876 1.00 23.20 ? 10   DG  L "O4'" 1 
ATOM   859   C  "C3'" . DG  H  2 6   ? 80.508  24.765  125.761 1.00 26.29 ? 10   DG  L "C3'" 1 
ATOM   860   O  "O3'" . DG  H  2 6   ? 79.241  24.684  126.422 1.00 23.83 ? 10   DG  L "O3'" 1 
ATOM   861   C  "C2'" . DG  H  2 6   ? 80.396  25.400  124.375 1.00 23.91 ? 10   DG  L "C2'" 1 
ATOM   862   C  "C1'" . DG  H  2 6   ? 80.265  26.885  124.694 1.00 26.74 ? 10   DG  L "C1'" 1 
ATOM   863   N  N9    . DG  H  2 6   ? 80.776  27.837  123.695 1.00 22.20 ? 10   DG  L N9    1 
ATOM   864   C  C8    . DG  H  2 6   ? 81.992  27.751  123.068 1.00 26.61 ? 10   DG  L C8    1 
ATOM   865   N  N7    . DG  H  2 6   ? 82.279  28.796  122.346 1.00 22.76 ? 10   DG  L N7    1 
ATOM   866   C  C5    . DG  H  2 6   ? 81.176  29.623  122.475 1.00 21.85 ? 10   DG  L C5    1 
ATOM   867   C  C6    . DG  H  2 6   ? 80.946  30.899  121.944 1.00 22.92 ? 10   DG  L C6    1 
ATOM   868   O  O6    . DG  H  2 6   ? 81.713  31.606  121.263 1.00 30.19 ? 10   DG  L O6    1 
ATOM   869   N  N1    . DG  H  2 6   ? 79.683  31.375  122.276 1.00 27.40 ? 10   DG  L N1    1 
ATOM   870   C  C2    . DG  H  2 6   ? 78.771  30.702  123.040 1.00 17.08 ? 10   DG  L C2    1 
ATOM   871   N  N2    . DG  H  2 6   ? 77.587  31.314  123.199 1.00 25.99 ? 10   DG  L N2    1 
ATOM   872   N  N3    . DG  H  2 6   ? 78.996  29.510  123.593 1.00 26.20 ? 10   DG  L N3    1 
ATOM   873   C  C4    . DG  H  2 6   ? 80.210  29.029  123.266 1.00 19.98 ? 10   DG  L C4    1 
ATOM   874   P  P     . DC  H  2 7   ? 78.219  23.484  126.108 1.00 26.00 ? 11   DC  L P     1 
ATOM   875   O  OP1   . DC  H  2 7   ? 77.703  23.023  127.427 1.00 27.55 ? 11   DC  L OP1   1 
ATOM   876   O  OP2   . DC  H  2 7   ? 78.859  22.496  125.203 1.00 28.00 ? 11   DC  L OP2   1 
ATOM   877   O  "O5'" . DC  H  2 7   ? 77.040  24.234  125.362 1.00 29.32 ? 11   DC  L "O5'" 1 
ATOM   878   C  "C5'" . DC  H  2 7   ? 76.396  25.343  125.985 1.00 34.50 ? 11   DC  L "C5'" 1 
ATOM   879   C  "C4'" . DC  H  2 7   ? 75.612  26.132  124.964 1.00 42.25 ? 11   DC  L "C4'" 1 
ATOM   880   O  "O4'" . DC  H  2 7   ? 76.506  26.809  124.041 1.00 40.80 ? 11   DC  L "O4'" 1 
ATOM   881   C  "C3'" . DC  H  2 7   ? 74.674  25.280  124.107 1.00 43.63 ? 11   DC  L "C3'" 1 
ATOM   882   O  "O3'" . DC  H  2 7   ? 73.384  25.896  124.099 1.00 50.57 ? 11   DC  L "O3'" 1 
ATOM   883   C  "C2'" . DC  H  2 7   ? 75.352  25.246  122.744 1.00 42.87 ? 11   DC  L "C2'" 1 
ATOM   884   C  "C1'" . DC  H  2 7   ? 76.074  26.584  122.702 1.00 41.87 ? 11   DC  L "C1'" 1 
ATOM   885   N  N1    . DC  H  2 7   ? 77.264  26.640  121.827 1.00 35.72 ? 11   DC  L N1    1 
ATOM   886   C  C2    . DC  H  2 7   ? 77.524  27.818  121.101 1.00 33.71 ? 11   DC  L C2    1 
ATOM   887   O  O2    . DC  H  2 7   ? 76.710  28.754  121.151 1.00 37.51 ? 11   DC  L O2    1 
ATOM   888   N  N3    . DC  H  2 7   ? 78.655  27.904  120.367 1.00 29.87 ? 11   DC  L N3    1 
ATOM   889   C  C4    . DC  H  2 7   ? 79.505  26.876  120.331 1.00 31.15 ? 11   DC  L C4    1 
ATOM   890   N  N4    . DC  H  2 7   ? 80.634  27.028  119.641 1.00 35.03 ? 11   DC  L N4    1 
ATOM   891   C  C5    . DC  H  2 7   ? 79.241  25.653  121.015 1.00 31.35 ? 11   DC  L C5    1 
ATOM   892   C  C6    . DC  H  2 7   ? 78.120  25.578  121.742 1.00 34.34 ? 11   DC  L C6    1 
ATOM   893   N  N     . MET I  3 1   ? 71.210  102.173 141.860 1.00 47.71 ? 1    MET A N     1 
ATOM   894   C  CA    . MET I  3 1   ? 71.620  101.462 140.609 1.00 47.78 ? 1    MET A CA    1 
ATOM   895   C  C     . MET I  3 1   ? 71.083  100.035 140.673 1.00 44.44 ? 1    MET A C     1 
ATOM   896   O  O     . MET I  3 1   ? 71.668  99.174  141.338 1.00 43.31 ? 1    MET A O     1 
ATOM   897   C  CB    . MET I  3 1   ? 73.154  101.426 140.499 1.00 51.86 ? 1    MET A CB    1 
ATOM   898   C  CG    . MET I  3 1   ? 73.765  102.093 139.256 1.00 56.36 ? 1    MET A CG    1 
ATOM   899   S  SD    . MET I  3 1   ? 73.684  101.111 137.718 1.00 60.04 ? 1    MET A SD    1 
ATOM   900   C  CE    . MET I  3 1   ? 73.107  102.353 136.525 1.00 60.03 ? 1    MET A CE    1 
ATOM   901   N  N     . GLN I  3 2   ? 69.956  99.793  140.017 1.00 40.87 ? 2    GLN A N     1 
ATOM   902   C  CA    . GLN I  3 2   ? 69.388  98.452  139.992 1.00 39.61 ? 2    GLN A CA    1 
ATOM   903   C  C     . GLN I  3 2   ? 70.177  97.693  138.923 1.00 34.39 ? 2    GLN A C     1 
ATOM   904   O  O     . GLN I  3 2   ? 70.439  98.222  137.852 1.00 32.00 ? 2    GLN A O     1 
ATOM   905   C  CB    . GLN I  3 2   ? 67.901  98.504  139.618 1.00 45.07 ? 2    GLN A CB    1 
ATOM   906   C  CG    . GLN I  3 2   ? 66.983  98.967  140.749 1.00 52.04 ? 2    GLN A CG    1 
ATOM   907   C  CD    . GLN I  3 2   ? 65.598  99.342  140.259 1.00 58.34 ? 2    GLN A CD    1 
ATOM   908   O  OE1   . GLN I  3 2   ? 65.171  98.912  139.182 1.00 60.03 ? 2    GLN A OE1   1 
ATOM   909   N  NE2   . GLN I  3 2   ? 64.879  100.141 141.054 1.00 60.03 ? 2    GLN A NE2   1 
ATOM   910   N  N     . PRO I  3 3   ? 70.607  96.464  139.224 1.00 32.31 ? 3    PRO A N     1 
ATOM   911   C  CA    . PRO I  3 3   ? 71.362  95.709  138.212 1.00 29.47 ? 3    PRO A CA    1 
ATOM   912   C  C     . PRO I  3 3   ? 70.516  95.473  136.963 1.00 27.31 ? 3    PRO A C     1 
ATOM   913   O  O     . PRO I  3 3   ? 69.294  95.579  137.010 1.00 26.89 ? 3    PRO A O     1 
ATOM   914   C  CB    . PRO I  3 3   ? 71.742  94.424  138.947 1.00 31.83 ? 3    PRO A CB    1 
ATOM   915   C  CG    . PRO I  3 3   ? 70.684  94.277  139.971 1.00 35.37 ? 3    PRO A CG    1 
ATOM   916   C  CD    . PRO I  3 3   ? 70.432  95.687  140.456 1.00 30.78 ? 3    PRO A CD    1 
ATOM   917   N  N     . LEU I  3 4   ? 71.151  95.153  135.838 1.00 25.09 ? 4    LEU A N     1 
ATOM   918   C  CA    . LEU I  3 4   ? 70.394  94.973  134.610 1.00 26.18 ? 4    LEU A CA    1 
ATOM   919   C  C     . LEU I  3 4   ? 69.376  93.846  134.604 1.00 23.24 ? 4    LEU A C     1 
ATOM   920   O  O     . LEU I  3 4   ? 68.360  93.973  133.940 1.00 23.33 ? 4    LEU A O     1 
ATOM   921   C  CB    . LEU I  3 4   ? 71.324  94.828  133.402 1.00 25.97 ? 4    LEU A CB    1 
ATOM   922   C  CG    . LEU I  3 4   ? 72.188  96.051  133.104 1.00 30.90 ? 4    LEU A CG    1 
ATOM   923   C  CD1   . LEU I  3 4   ? 72.912  95.828  131.778 1.00 29.16 ? 4    LEU A CD1   1 
ATOM   924   C  CD2   . LEU I  3 4   ? 71.327  97.313  133.040 1.00 33.06 ? 4    LEU A CD2   1 
ATOM   925   N  N     . PHE I  3 5   ? 69.641  92.751  135.312 1.00 24.15 ? 5    PHE A N     1 
ATOM   926   C  CA    . PHE I  3 5   ? 68.660  91.672  135.325 1.00 23.07 ? 5    PHE A CA    1 
ATOM   927   C  C     . PHE I  3 5   ? 67.414  92.101  136.103 1.00 22.64 ? 5    PHE A C     1 
ATOM   928   O  O     . PHE I  3 5   ? 66.313  91.625  135.819 1.00 21.25 ? 5    PHE A O     1 
ATOM   929   C  CB    . PHE I  3 5   ? 69.266  90.386  135.880 1.00 24.00 ? 5    PHE A CB    1 
ATOM   930   C  CG    . PHE I  3 5   ? 70.089  89.609  134.855 1.00 25.77 ? 5    PHE A CG    1 
ATOM   931   C  CD1   . PHE I  3 5   ? 70.684  88.401  135.192 1.00 29.65 ? 5    PHE A CD1   1 
ATOM   932   C  CD2   . PHE I  3 5   ? 70.254  90.094  133.560 1.00 23.51 ? 5    PHE A CD2   1 
ATOM   933   C  CE1   . PHE I  3 5   ? 71.439  87.686  134.245 1.00 31.58 ? 5    PHE A CE1   1 
ATOM   934   C  CE2   . PHE I  3 5   ? 70.997  89.390  132.614 1.00 25.67 ? 5    PHE A CE2   1 
ATOM   935   C  CZ    . PHE I  3 5   ? 71.585  88.190  132.958 1.00 24.99 ? 5    PHE A CZ    1 
ATOM   936   N  N     . THR I  3 6   ? 67.585  93.020  137.061 1.00 22.70 ? 6    THR A N     1 
ATOM   937   C  CA    . THR I  3 6   ? 66.434  93.513  137.815 1.00 24.87 ? 6    THR A CA    1 
ATOM   938   C  C     . THR I  3 6   ? 65.640  94.419  136.871 1.00 23.81 ? 6    THR A C     1 
ATOM   939   O  O     . THR I  3 6   ? 64.401  94.355  136.818 1.00 24.20 ? 6    THR A O     1 
ATOM   940   C  CB    . THR I  3 6   ? 66.886  94.292  139.076 1.00 23.46 ? 6    THR A CB    1 
ATOM   941   O  OG1   . THR I  3 6   ? 67.633  93.409  139.922 1.00 26.48 ? 6    THR A OG1   1 
ATOM   942   C  CG2   . THR I  3 6   ? 65.677  94.829  139.864 1.00 28.16 ? 6    THR A CG2   1 
ATOM   943   N  N     . GLN I  3 7   ? 66.349  95.233  136.092 1.00 25.07 ? 7    GLN A N     1 
ATOM   944   C  CA    . GLN I  3 7   ? 65.700  96.117  135.138 1.00 25.03 ? 7    GLN A CA    1 
ATOM   945   C  C     . GLN I  3 7   ? 64.938  95.294  134.090 1.00 26.83 ? 7    GLN A C     1 
ATOM   946   O  O     . GLN I  3 7   ? 63.806  95.619  133.723 1.00 25.29 ? 7    GLN A O     1 
ATOM   947   C  CB    . GLN I  3 7   ? 66.740  97.013  134.463 1.00 25.96 ? 7    GLN A CB    1 
ATOM   948   C  CG    . GLN I  3 7   ? 67.421  97.954  135.442 1.00 28.20 ? 7    GLN A CG    1 
ATOM   949   C  CD    . GLN I  3 7   ? 68.346  98.940  134.776 1.00 31.29 ? 7    GLN A CD    1 
ATOM   950   O  OE1   . GLN I  3 7   ? 68.016  99.512  133.733 1.00 35.20 ? 7    GLN A OE1   1 
ATOM   951   N  NE2   . GLN I  3 7   ? 69.510  99.162  135.384 1.00 35.08 ? 7    GLN A NE2   1 
ATOM   952   N  N     . GLU I  3 8   ? 65.556  94.213  133.619 1.00 24.15 ? 8    GLU A N     1 
ATOM   953   C  CA    . GLU I  3 8   ? 64.906  93.361  132.621 1.00 24.97 ? 8    GLU A CA    1 
ATOM   954   C  C     . GLU I  3 8   ? 63.655  92.691  133.195 1.00 20.73 ? 8    GLU A C     1 
ATOM   955   O  O     . GLU I  3 8   ? 62.667  92.522  132.498 1.00 22.87 ? 8    GLU A O     1 
ATOM   956   C  CB    . GLU I  3 8   ? 65.863  92.276  132.137 1.00 27.54 ? 8    GLU A CB    1 
ATOM   957   C  CG    . GLU I  3 8   ? 66.965  92.773  131.223 1.00 36.05 ? 8    GLU A CG    1 
ATOM   958   C  CD    . GLU I  3 8   ? 66.443  93.289  129.895 1.00 39.13 ? 8    GLU A CD    1 
ATOM   959   O  OE1   . GLU I  3 8   ? 65.431  92.749  129.393 1.00 37.54 ? 8    GLU A OE1   1 
ATOM   960   O  OE2   . GLU I  3 8   ? 67.061  94.226  129.343 1.00 45.25 ? 8    GLU A OE2   1 
ATOM   961   N  N     . ARG I  3 9   ? 63.725  92.284  134.459 1.00 20.52 ? 9    ARG A N     1 
ATOM   962   C  CA    . ARG I  3 9   ? 62.588  91.637  135.116 1.00 19.92 ? 9    ARG A CA    1 
ATOM   963   C  C     . ARG I  3 9   ? 61.429  92.627  135.213 1.00 21.63 ? 9    ARG A C     1 
ATOM   964   O  O     . ARG I  3 9   ? 60.270  92.260  135.004 1.00 22.85 ? 9    ARG A O     1 
ATOM   965   C  CB    . ARG I  3 9   ? 62.999  91.152  136.516 1.00 20.53 ? 9    ARG A CB    1 
ATOM   966   C  CG    . ARG I  3 9   ? 61.954  90.299  137.241 1.00 19.00 ? 9    ARG A CG    1 
ATOM   967   C  CD    . ARG I  3 9   ? 62.457  89.938  138.615 1.00 20.87 ? 9    ARG A CD    1 
ATOM   968   N  NE    . ARG I  3 9   ? 61.610  88.992  139.331 1.00 20.04 ? 9    ARG A NE    1 
ATOM   969   C  CZ    . ARG I  3 9   ? 60.632  89.335  140.171 1.00 25.86 ? 9    ARG A CZ    1 
ATOM   970   N  NH1   . ARG I  3 9   ? 60.363  90.615  140.408 1.00 23.10 ? 9    ARG A NH1   1 
ATOM   971   N  NH2   . ARG I  3 9   ? 59.938  88.391  140.787 1.00 19.06 ? 9    ARG A NH2   1 
ATOM   972   N  N     . ARG I  3 10  ? 61.742  93.887  135.500 1.00 21.58 ? 10   ARG A N     1 
ATOM   973   C  CA    . ARG I  3 10  ? 60.683  94.897  135.585 1.00 24.65 ? 10   ARG A CA    1 
ATOM   974   C  C     . ARG I  3 10  ? 60.077  95.170  134.218 1.00 22.31 ? 10   ARG A C     1 
ATOM   975   O  O     . ARG I  3 10  ? 58.876  95.360  134.088 1.00 26.37 ? 10   ARG A O     1 
ATOM   976   C  CB    . ARG I  3 10  ? 61.240  96.184  136.216 1.00 26.65 ? 10   ARG A CB    1 
ATOM   977   C  CG    . ARG I  3 10  ? 61.695  95.924  137.638 1.00 35.91 ? 10   ARG A CG    1 
ATOM   978   C  CD    . ARG I  3 10  ? 62.191  97.155  138.391 1.00 42.20 ? 10   ARG A CD    1 
ATOM   979   N  NE    . ARG I  3 10  ? 62.651  96.774  139.728 1.00 44.94 ? 10   ARG A NE    1 
ATOM   980   C  CZ    . ARG I  3 10  ? 62.928  97.635  140.702 1.00 49.08 ? 10   ARG A CZ    1 
ATOM   981   N  NH1   . ARG I  3 10  ? 62.791  98.940  140.499 1.00 50.12 ? 10   ARG A NH1   1 
ATOM   982   N  NH2   . ARG I  3 10  ? 63.346  97.191  141.883 1.00 51.54 ? 10   ARG A NH2   1 
ATOM   983   N  N     . ILE I  3 11  ? 60.907  95.169  133.182 1.00 22.25 ? 11   ILE A N     1 
ATOM   984   C  CA    . ILE I  3 11  ? 60.423  95.382  131.832 1.00 23.19 ? 11   ILE A CA    1 
ATOM   985   C  C     . ILE I  3 11  ? 59.472  94.247  131.450 1.00 21.83 ? 11   ILE A C     1 
ATOM   986   O  O     . ILE I  3 11  ? 58.460  94.464  130.791 1.00 22.15 ? 11   ILE A O     1 
ATOM   987   C  CB    . ILE I  3 11  ? 61.616  95.453  130.840 1.00 23.30 ? 11   ILE A CB    1 
ATOM   988   C  CG1   . ILE I  3 11  ? 62.379  96.770  131.058 1.00 25.36 ? 11   ILE A CG1   1 
ATOM   989   C  CG2   . ILE I  3 11  ? 61.133  95.318  129.405 1.00 23.74 ? 11   ILE A CG2   1 
ATOM   990   C  CD1   . ILE I  3 11  ? 63.701  96.855  130.304 1.00 28.62 ? 11   ILE A CD1   1 
ATOM   991   N  N     . PHE I  3 12  ? 59.818  93.030  131.858 1.00 20.13 ? 12   PHE A N     1 
ATOM   992   C  CA    . PHE I  3 12  ? 59.005  91.845  131.599 1.00 18.90 ? 12   PHE A CA    1 
ATOM   993   C  C     . PHE I  3 12  ? 57.606  92.050  132.238 1.00 18.62 ? 12   PHE A C     1 
ATOM   994   O  O     . PHE I  3 12  ? 56.577  91.869  131.591 1.00 20.95 ? 12   PHE A O     1 
ATOM   995   C  CB    . PHE I  3 12  ? 59.765  90.642  132.191 1.00 19.97 ? 12   PHE A CB    1 
ATOM   996   C  CG    . PHE I  3 12  ? 58.946  89.390  132.371 1.00 18.37 ? 12   PHE A CG    1 
ATOM   997   C  CD1   . PHE I  3 12  ? 58.619  88.573  131.291 1.00 18.00 ? 12   PHE A CD1   1 
ATOM   998   C  CD2   . PHE I  3 12  ? 58.577  88.987  133.649 1.00 19.62 ? 12   PHE A CD2   1 
ATOM   999   C  CE1   . PHE I  3 12  ? 57.933  87.365  131.475 1.00 18.29 ? 12   PHE A CE1   1 
ATOM   1000  C  CE2   . PHE I  3 12  ? 57.887  87.770  133.853 1.00 18.28 ? 12   PHE A CE2   1 
ATOM   1001  C  CZ    . PHE I  3 12  ? 57.572  86.969  132.759 1.00 20.21 ? 12   PHE A CZ    1 
ATOM   1002  N  N     . HIS I  3 13  ? 57.582  92.455  133.508 1.00 19.53 ? 13   HIS A N     1 
ATOM   1003  C  CA    . HIS I  3 13  ? 56.300  92.677  134.178 1.00 20.65 ? 13   HIS A CA    1 
ATOM   1004  C  C     . HIS I  3 13  ? 55.510  93.805  133.518 1.00 19.30 ? 13   HIS A C     1 
ATOM   1005  O  O     . HIS I  3 13  ? 54.289  93.709  133.340 1.00 19.19 ? 13   HIS A O     1 
ATOM   1006  C  CB    . HIS I  3 13  ? 56.530  92.997  135.653 1.00 19.62 ? 13   HIS A CB    1 
ATOM   1007  C  CG    . HIS I  3 13  ? 56.937  91.812  136.466 1.00 21.01 ? 13   HIS A CG    1 
ATOM   1008  N  ND1   . HIS I  3 13  ? 57.626  91.924  137.655 1.00 22.47 ? 13   HIS A ND1   1 
ATOM   1009  C  CD2   . HIS I  3 13  ? 56.735  90.489  136.267 1.00 18.99 ? 13   HIS A CD2   1 
ATOM   1010  C  CE1   . HIS I  3 13  ? 57.835  90.717  138.152 1.00 21.55 ? 13   HIS A CE1   1 
ATOM   1011  N  NE2   . HIS I  3 13  ? 57.302  89.829  137.330 1.00 18.31 ? 13   HIS A NE2   1 
ATOM   1012  N  N     . LYS I  3 14  ? 56.211  94.868  133.138 1.00 22.29 ? 14   LYS A N     1 
ATOM   1013  C  CA    . LYS I  3 14  ? 55.552  96.006  132.509 1.00 24.62 ? 14   LYS A CA    1 
ATOM   1014  C  C     . LYS I  3 14  ? 54.858  95.631  131.205 1.00 23.79 ? 14   LYS A C     1 
ATOM   1015  O  O     . LYS I  3 14  ? 53.787  96.148  130.900 1.00 24.09 ? 14   LYS A O     1 
ATOM   1016  C  CB    . LYS I  3 14  ? 56.555  97.139  132.281 1.00 25.47 ? 14   LYS A CB    1 
ATOM   1017  C  CG    . LYS I  3 14  ? 55.934  98.445  131.823 1.00 36.20 ? 14   LYS A CG    1 
ATOM   1018  C  CD    . LYS I  3 14  ? 56.976  99.561  131.804 1.00 40.96 ? 14   LYS A CD    1 
ATOM   1019  C  CE    . LYS I  3 14  ? 56.362  100.900 131.394 1.00 46.42 ? 14   LYS A CE    1 
ATOM   1020  N  NZ    . LYS I  3 14  ? 55.941  100.922 129.960 1.00 47.83 ? 14   LYS A NZ    1 
ATOM   1021  N  N     . LYS I  3 15  ? 55.449  94.732  130.422 1.00 21.65 ? 15   LYS A N     1 
ATOM   1022  C  CA    . LYS I  3 15  ? 54.806  94.315  129.189 1.00 21.85 ? 15   LYS A CA    1 
ATOM   1023  C  C     . LYS I  3 15  ? 53.510  93.559  129.485 1.00 19.22 ? 15   LYS A C     1 
ATOM   1024  O  O     . LYS I  3 15  ? 52.515  93.678  128.759 1.00 21.31 ? 15   LYS A O     1 
ATOM   1025  C  CB    . LYS I  3 15  ? 55.752  93.423  128.378 1.00 21.85 ? 15   LYS A CB    1 
ATOM   1026  C  CG    . LYS I  3 15  ? 56.987  94.156  127.879 1.00 22.78 ? 15   LYS A CG    1 
ATOM   1027  C  CD    . LYS I  3 15  ? 57.862  93.207  127.041 1.00 22.12 ? 15   LYS A CD    1 
ATOM   1028  C  CE    . LYS I  3 15  ? 59.094  93.918  126.493 1.00 28.47 ? 15   LYS A CE    1 
ATOM   1029  N  NZ    . LYS I  3 15  ? 59.992  92.945  125.779 1.00 28.38 ? 15   LYS A NZ    1 
ATOM   1030  N  N     . LEU I  3 16  ? 53.529  92.765  130.554 1.00 20.63 ? 16   LEU A N     1 
ATOM   1031  C  CA    . LEU I  3 16  ? 52.341  92.020  130.928 1.00 20.04 ? 16   LEU A CA    1 
ATOM   1032  C  C     . LEU I  3 16  ? 51.262  93.013  131.377 1.00 20.04 ? 16   LEU A C     1 
ATOM   1033  O  O     . LEU I  3 16  ? 50.092  92.803  131.105 1.00 22.12 ? 16   LEU A O     1 
ATOM   1034  C  CB    . LEU I  3 16  ? 52.653  91.029  132.062 1.00 17.12 ? 16   LEU A CB    1 
ATOM   1035  C  CG    . LEU I  3 16  ? 53.568  89.847  131.696 1.00 18.41 ? 16   LEU A CG    1 
ATOM   1036  C  CD1   . LEU I  3 16  ? 53.859  89.036  132.945 1.00 21.83 ? 16   LEU A CD1   1 
ATOM   1037  C  CD2   . LEU I  3 16  ? 52.917  88.980  130.625 1.00 20.62 ? 16   LEU A CD2   1 
ATOM   1038  N  N     . LEU I  3 17  ? 51.662  94.079  132.066 1.00 20.63 ? 17   LEU A N     1 
ATOM   1039  C  CA    . LEU I  3 17  ? 50.680  95.070  132.508 1.00 21.82 ? 17   LEU A CA    1 
ATOM   1040  C  C     . LEU I  3 17  ? 50.172  95.905  131.336 1.00 24.36 ? 17   LEU A C     1 
ATOM   1041  O  O     . LEU I  3 17  ? 48.963  96.046  131.136 1.00 25.03 ? 17   LEU A O     1 
ATOM   1042  C  CB    . LEU I  3 17  ? 51.285  96.009  133.567 1.00 22.64 ? 17   LEU A CB    1 
ATOM   1043  C  CG    . LEU I  3 17  ? 51.732  95.355  134.866 1.00 27.21 ? 17   LEU A CG    1 
ATOM   1044  C  CD1   . LEU I  3 17  ? 52.272  96.432  135.820 1.00 29.83 ? 17   LEU A CD1   1 
ATOM   1045  C  CD2   . LEU I  3 17  ? 50.556  94.627  135.491 1.00 30.00 ? 17   LEU A CD2   1 
ATOM   1046  N  N     . ASP I  3 18  ? 51.095  96.449  130.549 1.00 26.40 ? 18   ASP A N     1 
ATOM   1047  C  CA    . ASP I  3 18  ? 50.702  97.297  129.428 1.00 26.35 ? 18   ASP A CA    1 
ATOM   1048  C  C     . ASP I  3 18  ? 49.803  96.591  128.414 1.00 24.95 ? 18   ASP A C     1 
ATOM   1049  O  O     . ASP I  3 18  ? 48.945  97.221  127.799 1.00 25.06 ? 18   ASP A O     1 
ATOM   1050  C  CB    . ASP I  3 18  ? 51.947  97.875  128.725 1.00 28.16 ? 18   ASP A CB    1 
ATOM   1051  C  CG    . ASP I  3 18  ? 52.704  98.897  129.580 1.00 30.32 ? 18   ASP A CG    1 
ATOM   1052  O  OD1   . ASP I  3 18  ? 52.270  99.244  130.704 1.00 34.57 ? 18   ASP A OD1   1 
ATOM   1053  O  OD2   . ASP I  3 18  ? 53.764  99.368  129.113 1.00 35.29 ? 18   ASP A OD2   1 
ATOM   1054  N  N     . GLY I  3 19  ? 49.982  95.286  128.233 1.00 24.23 ? 19   GLY A N     1 
ATOM   1055  C  CA    . GLY I  3 19  ? 49.155  94.563  127.287 1.00 23.94 ? 19   GLY A CA    1 
ATOM   1056  C  C     . GLY I  3 19  ? 47.859  94.064  127.907 1.00 24.96 ? 19   GLY A C     1 
ATOM   1057  O  O     . GLY I  3 19  ? 47.059  93.392  127.256 1.00 27.26 ? 19   GLY A O     1 
ATOM   1058  N  N     . ASN I  3 20  ? 47.652  94.406  129.178 1.00 26.62 ? 20   ASN A N     1 
ATOM   1059  C  CA    . ASN I  3 20  ? 46.466  93.969  129.921 1.00 26.96 ? 20   ASN A CA    1 
ATOM   1060  C  C     . ASN I  3 20  ? 46.416  92.441  130.068 1.00 24.53 ? 20   ASN A C     1 
ATOM   1061  O  O     . ASN I  3 20  ? 45.335  91.867  130.248 1.00 23.16 ? 20   ASN A O     1 
ATOM   1062  C  CB    . ASN I  3 20  ? 45.182  94.479  129.244 1.00 27.83 ? 20   ASN A CB    1 
ATOM   1063  C  CG    . ASN I  3 20  ? 45.019  95.984  129.360 1.00 28.79 ? 20   ASN A CG    1 
ATOM   1064  O  OD1   . ASN I  3 20  ? 44.100  96.565  128.786 1.00 37.86 ? 20   ASN A OD1   1 
ATOM   1065  N  ND2   . ASN I  3 20  ? 45.908  96.619  130.100 1.00 30.20 ? 20   ASN A ND2   1 
ATOM   1066  N  N     . ILE I  3 21  ? 47.580  91.790  129.969 1.00 23.09 ? 21   ILE A N     1 
ATOM   1067  C  CA    . ILE I  3 21  ? 47.656  90.333  130.115 1.00 24.13 ? 21   ILE A CA    1 
ATOM   1068  C  C     . ILE I  3 21  ? 47.391  90.073  131.591 1.00 21.17 ? 21   ILE A C     1 
ATOM   1069  O  O     . ILE I  3 21  ? 46.605  89.192  131.949 1.00 22.70 ? 21   ILE A O     1 
ATOM   1070  C  CB    . ILE I  3 21  ? 49.047  89.787  129.741 1.00 24.95 ? 21   ILE A CB    1 
ATOM   1071  C  CG1   . ILE I  3 21  ? 49.428  90.239  128.309 1.00 26.72 ? 21   ILE A CG1   1 
ATOM   1072  C  CG2   . ILE I  3 21  ? 49.051  88.270  129.894 1.00 23.88 ? 21   ILE A CG2   1 
ATOM   1073  C  CD1   . ILE I  3 21  ? 48.315  90.103  127.296 1.00 29.25 ? 21   ILE A CD1   1 
ATOM   1074  N  N     . LEU I  3 22  ? 48.073  90.850  132.432 1.00 22.38 ? 22   LEU A N     1 
ATOM   1075  C  CA    . LEU I  3 22  ? 47.886  90.807  133.883 1.00 21.10 ? 22   LEU A CA    1 
ATOM   1076  C  C     . LEU I  3 22  ? 47.107  92.084  134.236 1.00 21.29 ? 22   LEU A C     1 
ATOM   1077  O  O     . LEU I  3 22  ? 47.619  93.194  134.067 1.00 22.56 ? 22   LEU A O     1 
ATOM   1078  C  CB    . LEU I  3 22  ? 49.220  90.830  134.640 1.00 21.66 ? 22   LEU A CB    1 
ATOM   1079  C  CG    . LEU I  3 22  ? 49.040  90.794  136.174 1.00 23.17 ? 22   LEU A CG    1 
ATOM   1080  C  CD1   . LEU I  3 22  ? 48.414  89.452  136.601 1.00 24.40 ? 22   LEU A CD1   1 
ATOM   1081  C  CD2   . LEU I  3 22  ? 50.373  90.978  136.864 1.00 23.62 ? 22   LEU A CD2   1 
ATOM   1082  N  N     . ALA I  3 23  ? 45.875  91.926  134.709 1.00 18.53 ? 23   ALA A N     1 
ATOM   1083  C  CA    . ALA I  3 23  ? 45.056  93.095  135.073 1.00 18.75 ? 23   ALA A CA    1 
ATOM   1084  C  C     . ALA I  3 23  ? 43.957  92.616  136.006 1.00 21.53 ? 23   ALA A C     1 
ATOM   1085  O  O     . ALA I  3 23  ? 43.940  91.446  136.397 1.00 20.70 ? 23   ALA A O     1 
ATOM   1086  C  CB    . ALA I  3 23  ? 44.459  93.729  133.832 1.00 21.65 ? 23   ALA A CB    1 
ATOM   1087  N  N     . THR I  3 24  ? 43.047  93.516  136.367 1.00 21.80 ? 24   THR A N     1 
ATOM   1088  C  CA    . THR I  3 24  ? 41.961  93.173  137.290 1.00 24.15 ? 24   THR A CA    1 
ATOM   1089  C  C     . THR I  3 24  ? 40.643  93.494  136.603 1.00 21.25 ? 24   THR A C     1 
ATOM   1090  O  O     . THR I  3 24  ? 40.541  94.534  135.951 1.00 21.24 ? 24   THR A O     1 
ATOM   1091  C  CB    . THR I  3 24  ? 42.073  94.021  138.588 1.00 23.31 ? 24   THR A CB    1 
ATOM   1092  O  OG1   . THR I  3 24  ? 43.361  93.825  139.190 1.00 25.00 ? 24   THR A OG1   1 
ATOM   1093  C  CG2   . THR I  3 24  ? 40.999  93.646  139.575 1.00 23.37 ? 24   THR A CG2   1 
ATOM   1094  N  N     . ASN I  3 25  ? 39.641  92.612  136.704 1.00 20.83 ? 25   ASN A N     1 
ATOM   1095  C  CA    . ASN I  3 25  ? 38.373  92.950  136.056 1.00 21.03 ? 25   ASN A CA    1 
ATOM   1096  C  C     . ASN I  3 25  ? 37.488  93.762  137.003 1.00 21.32 ? 25   ASN A C     1 
ATOM   1097  O  O     . ASN I  3 25  ? 37.881  94.043  138.143 1.00 21.16 ? 25   ASN A O     1 
ATOM   1098  C  CB    . ASN I  3 25  ? 37.626  91.712  135.514 1.00 20.15 ? 25   ASN A CB    1 
ATOM   1099  C  CG    . ASN I  3 25  ? 37.076  90.793  136.595 1.00 22.70 ? 25   ASN A CG    1 
ATOM   1100  O  OD1   . ASN I  3 25  ? 37.026  91.126  137.771 1.00 22.70 ? 25   ASN A OD1   1 
ATOM   1101  N  ND2   . ASN I  3 25  ? 36.634  89.618  136.171 1.00 25.14 ? 25   ASN A ND2   1 
ATOM   1102  N  N     . ASN I  3 26  ? 36.303  94.143  136.541 1.00 22.12 ? 26   ASN A N     1 
ATOM   1103  C  CA    . ASN I  3 26  ? 35.428  94.963  137.379 1.00 22.58 ? 26   ASN A CA    1 
ATOM   1104  C  C     . ASN I  3 26  ? 34.754  94.257  138.565 1.00 26.16 ? 26   ASN A C     1 
ATOM   1105  O  O     . ASN I  3 26  ? 33.921  94.868  139.256 1.00 25.38 ? 26   ASN A O     1 
ATOM   1106  C  CB    . ASN I  3 26  ? 34.389  95.692  136.512 1.00 25.70 ? 26   ASN A CB    1 
ATOM   1107  C  CG    . ASN I  3 26  ? 33.423  94.763  135.824 1.00 25.94 ? 26   ASN A CG    1 
ATOM   1108  O  OD1   . ASN I  3 26  ? 33.305  93.588  136.164 1.00 29.76 ? 26   ASN A OD1   1 
ATOM   1109  N  ND2   . ASN I  3 26  ? 32.699  95.301  134.840 1.00 28.94 ? 26   ASN A ND2   1 
ATOM   1110  N  N     . ARG I  3 27  ? 35.096  92.987  138.793 1.00 23.39 ? 27   ARG A N     1 
ATOM   1111  C  CA    . ARG I  3 27  ? 34.570  92.231  139.935 1.00 25.70 ? 27   ARG A CA    1 
ATOM   1112  C  C     . ARG I  3 27  ? 35.738  91.935  140.887 1.00 25.07 ? 27   ARG A C     1 
ATOM   1113  O  O     . ARG I  3 27  ? 35.621  91.158  141.835 1.00 29.32 ? 27   ARG A O     1 
ATOM   1114  C  CB    . ARG I  3 27  ? 33.907  90.930  139.482 1.00 25.11 ? 27   ARG A CB    1 
ATOM   1115  C  CG    . ARG I  3 27  ? 32.667  91.172  138.670 1.00 27.67 ? 27   ARG A CG    1 
ATOM   1116  C  CD    . ARG I  3 27  ? 31.960  89.880  138.275 1.00 32.18 ? 27   ARG A CD    1 
ATOM   1117  N  NE    . ARG I  3 27  ? 30.914  90.198  137.308 1.00 39.63 ? 27   ARG A NE    1 
ATOM   1118  C  CZ    . ARG I  3 27  ? 29.695  90.630  137.624 1.00 44.50 ? 27   ARG A CZ    1 
ATOM   1119  N  NH1   . ARG I  3 27  ? 29.338  90.781  138.901 1.00 44.21 ? 27   ARG A NH1   1 
ATOM   1120  N  NH2   . ARG I  3 27  ? 28.851  90.968  136.660 1.00 48.45 ? 27   ARG A NH2   1 
ATOM   1121  N  N     . GLY I  3 28  ? 36.875  92.562  140.610 1.00 22.29 ? 28   GLY A N     1 
ATOM   1122  C  CA    . GLY I  3 28  ? 38.035  92.413  141.464 1.00 23.71 ? 28   GLY A CA    1 
ATOM   1123  C  C     . GLY I  3 28  ? 38.918  91.192  141.259 1.00 24.34 ? 28   GLY A C     1 
ATOM   1124  O  O     . GLY I  3 28  ? 39.857  90.981  142.028 1.00 26.95 ? 28   GLY A O     1 
ATOM   1125  N  N     . VAL I  3 29  ? 38.639  90.399  140.228 1.00 20.75 ? 29   VAL A N     1 
ATOM   1126  C  CA    . VAL I  3 29  ? 39.434  89.189  139.969 1.00 24.10 ? 29   VAL A CA    1 
ATOM   1127  C  C     . VAL I  3 29  ? 40.651  89.480  139.088 1.00 20.28 ? 29   VAL A C     1 
ATOM   1128  O  O     . VAL I  3 29  ? 40.505  90.018  137.985 1.00 20.88 ? 29   VAL A O     1 
ATOM   1129  C  CB    . VAL I  3 29  ? 38.610  88.112  139.232 1.00 24.53 ? 29   VAL A CB    1 
ATOM   1130  C  CG1   . VAL I  3 29  ? 39.426  86.819  139.150 1.00 24.69 ? 29   VAL A CG1   1 
ATOM   1131  C  CG2   . VAL I  3 29  ? 37.266  87.860  139.950 1.00 26.16 ? 29   VAL A CG2   1 
ATOM   1132  N  N     . VAL I  3 30  ? 41.841  89.130  139.572 1.00 22.17 ? 30   VAL A N     1 
ATOM   1133  C  CA    . VAL I  3 30  ? 43.062  89.347  138.794 1.00 20.85 ? 30   VAL A CA    1 
ATOM   1134  C  C     . VAL I  3 30  ? 43.114  88.256  137.721 1.00 22.54 ? 30   VAL A C     1 
ATOM   1135  O  O     . VAL I  3 30  ? 42.717  87.112  137.960 1.00 21.58 ? 30   VAL A O     1 
ATOM   1136  C  CB    . VAL I  3 30  ? 44.286  89.358  139.722 1.00 23.30 ? 30   VAL A CB    1 
ATOM   1137  C  CG1   . VAL I  3 30  ? 45.587  89.452  138.915 1.00 22.82 ? 30   VAL A CG1   1 
ATOM   1138  C  CG2   . VAL I  3 30  ? 44.164  90.576  140.638 1.00 23.68 ? 30   VAL A CG2   1 
ATOM   1139  N  N     . SER I  3 31  ? 43.585  88.625  136.532 1.00 20.32 ? 31   SER A N     1 
ATOM   1140  C  CA    . SER I  3 31  ? 43.565  87.743  135.373 1.00 20.13 ? 31   SER A CA    1 
ATOM   1141  C  C     . SER I  3 31  ? 44.327  86.426  135.375 1.00 21.71 ? 31   SER A C     1 
ATOM   1142  O  O     . SER I  3 31  ? 44.158  85.633  134.447 1.00 22.32 ? 31   SER A O     1 
ATOM   1143  C  CB    . SER I  3 31  ? 43.936  88.528  134.119 1.00 21.75 ? 31   SER A CB    1 
ATOM   1144  O  OG    . SER I  3 31  ? 45.238  89.031  134.256 1.00 21.50 ? 31   SER A OG    1 
ATOM   1145  N  N     . ASN I  3 32  ? 45.173  86.184  136.373 1.00 19.41 ? 32   ASN A N     1 
ATOM   1146  C  CA    . ASN I  3 32  ? 45.827  84.877  136.414 1.00 20.80 ? 32   ASN A CA    1 
ATOM   1147  C  C     . ASN I  3 32  ? 45.254  84.073  137.590 1.00 23.34 ? 32   ASN A C     1 
ATOM   1148  O  O     . ASN I  3 32  ? 45.736  82.986  137.915 1.00 23.92 ? 32   ASN A O     1 
ATOM   1149  C  CB    . ASN I  3 32  ? 47.368  84.997  136.496 1.00 19.10 ? 32   ASN A CB    1 
ATOM   1150  C  CG    . ASN I  3 32  ? 47.837  85.718  137.720 1.00 20.89 ? 32   ASN A CG    1 
ATOM   1151  O  OD1   . ASN I  3 32  ? 47.133  86.580  138.257 1.00 19.09 ? 32   ASN A OD1   1 
ATOM   1152  N  ND2   . ASN I  3 32  ? 49.043  85.387  138.180 1.00 20.35 ? 32   ASN A ND2   1 
ATOM   1153  N  N     . ALA I  3 33  ? 44.202  84.612  138.218 1.00 21.50 ? 33   ALA A N     1 
ATOM   1154  C  CA    . ALA I  3 33  ? 43.556  83.922  139.338 1.00 23.39 ? 33   ALA A CA    1 
ATOM   1155  C  C     . ALA I  3 33  ? 42.412  83.017  138.889 1.00 22.11 ? 33   ALA A C     1 
ATOM   1156  O  O     . ALA I  3 33  ? 41.891  83.142  137.790 1.00 24.11 ? 33   ALA A O     1 
ATOM   1157  C  CB    . ALA I  3 33  ? 42.999  84.952  140.344 1.00 22.94 ? 33   ALA A CB    1 
ATOM   1158  N  N     . ASP I  3 34  ? 42.041  82.090  139.769 1.00 22.75 ? 34   ASP A N     1 
ATOM   1159  C  CA    . ASP I  3 34  ? 40.913  81.202  139.549 1.00 24.46 ? 34   ASP A CA    1 
ATOM   1160  C  C     . ASP I  3 34  ? 39.925  81.792  140.569 1.00 23.92 ? 34   ASP A C     1 
ATOM   1161  O  O     . ASP I  3 34  ? 40.068  81.558  141.762 1.00 25.73 ? 34   ASP A O     1 
ATOM   1162  C  CB    . ASP I  3 34  ? 41.292  79.760  139.935 1.00 21.73 ? 34   ASP A CB    1 
ATOM   1163  C  CG    . ASP I  3 34  ? 40.093  78.816  139.949 1.00 26.58 ? 34   ASP A CG    1 
ATOM   1164  O  OD1   . ASP I  3 34  ? 38.955  79.284  139.716 1.00 25.03 ? 34   ASP A OD1   1 
ATOM   1165  O  OD2   . ASP I  3 34  ? 40.286  77.613  140.210 1.00 25.86 ? 34   ASP A OD2   1 
ATOM   1166  N  N     . GLY I  3 35  ? 38.943  82.567  140.099 1.00 25.62 ? 35   GLY A N     1 
ATOM   1167  C  CA    . GLY I  3 35  ? 37.993  83.208  141.006 1.00 27.28 ? 35   GLY A CA    1 
ATOM   1168  C  C     . GLY I  3 35  ? 37.175  82.344  141.952 1.00 28.79 ? 35   GLY A C     1 
ATOM   1169  O  O     . GLY I  3 35  ? 36.576  82.845  142.904 1.00 29.52 ? 35   GLY A O     1 
ATOM   1170  N  N     . SER I  3 36  ? 37.150  81.044  141.707 1.00 28.17 ? 36   SER A N     1 
ATOM   1171  C  CA    . SER I  3 36  ? 36.376  80.129  142.541 1.00 29.36 ? 36   SER A CA    1 
ATOM   1172  C  C     . SER I  3 36  ? 37.161  79.705  143.770 1.00 30.98 ? 36   SER A C     1 
ATOM   1173  O  O     . SER I  3 36  ? 36.657  78.954  144.621 1.00 31.69 ? 36   SER A O     1 
ATOM   1174  C  CB    . SER I  3 36  ? 36.025  78.882  141.723 1.00 31.54 ? 36   SER A CB    1 
ATOM   1175  O  OG    . SER I  3 36  ? 37.149  77.999  141.678 1.00 30.91 ? 36   SER A OG    1 
ATOM   1176  N  N     . ASN I  3 37  ? 38.399  80.179  143.874 1.00 27.39 ? 37   ASN A N     1 
ATOM   1177  C  CA    . ASN I  3 37  ? 39.244  79.778  144.993 1.00 29.00 ? 37   ASN A CA    1 
ATOM   1178  C  C     . ASN I  3 37  ? 39.761  80.986  145.742 1.00 29.30 ? 37   ASN A C     1 
ATOM   1179  O  O     . ASN I  3 37  ? 40.477  81.806  145.166 1.00 27.84 ? 37   ASN A O     1 
ATOM   1180  C  CB    . ASN I  3 37  ? 40.412  78.929  144.464 1.00 29.55 ? 37   ASN A CB    1 
ATOM   1181  C  CG    . ASN I  3 37  ? 41.262  78.348  145.577 1.00 32.02 ? 37   ASN A CG    1 
ATOM   1182  O  OD1   . ASN I  3 37  ? 42.279  78.922  145.969 1.00 33.04 ? 37   ASN A OD1   1 
ATOM   1183  N  ND2   . ASN I  3 37  ? 40.832  77.209  146.113 1.00 34.76 ? 37   ASN A ND2   1 
ATOM   1184  N  N     . THR I  3 38  ? 39.382  81.078  147.016 1.00 29.53 ? 38   THR A N     1 
ATOM   1185  C  CA    . THR I  3 38  ? 39.759  82.183  147.903 1.00 28.68 ? 38   THR A CA    1 
ATOM   1186  C  C     . THR I  3 38  ? 41.260  82.436  147.921 1.00 27.35 ? 38   THR A C     1 
ATOM   1187  O  O     . THR I  3 38  ? 41.712  83.577  147.785 1.00 26.56 ? 38   THR A O     1 
ATOM   1188  C  CB    . THR I  3 38  ? 39.301  81.912  149.374 1.00 31.77 ? 38   THR A CB    1 
ATOM   1189  O  OG1   . THR I  3 38  ? 37.874  81.773  149.415 1.00 36.24 ? 38   THR A OG1   1 
ATOM   1190  C  CG2   . THR I  3 38  ? 39.710  83.057  150.302 1.00 29.74 ? 38   THR A CG2   1 
ATOM   1191  N  N     . ARG I  3 39  ? 42.046  81.378  148.105 1.00 27.44 ? 39   ARG A N     1 
ATOM   1192  C  CA    . ARG I  3 39  ? 43.480  81.584  148.167 1.00 25.87 ? 39   ARG A CA    1 
ATOM   1193  C  C     . ARG I  3 39  ? 44.056  82.025  146.814 1.00 24.98 ? 39   ARG A C     1 
ATOM   1194  O  O     . ARG I  3 39  ? 44.925  82.896  146.778 1.00 23.29 ? 39   ARG A O     1 
ATOM   1195  C  CB    . ARG I  3 39  ? 44.173  80.326  148.713 1.00 30.42 ? 39   ARG A CB    1 
ATOM   1196  C  CG    . ARG I  3 39  ? 43.811  80.035  150.192 1.00 36.70 ? 39   ARG A CG    1 
ATOM   1197  C  CD    . ARG I  3 39  ? 44.638  78.892  150.763 1.00 37.71 ? 39   ARG A CD    1 
ATOM   1198  N  NE    . ARG I  3 39  ? 44.363  78.652  152.179 1.00 43.09 ? 39   ARG A NE    1 
ATOM   1199  C  CZ    . ARG I  3 39  ? 43.254  78.082  152.646 1.00 46.78 ? 39   ARG A CZ    1 
ATOM   1200  N  NH1   . ARG I  3 39  ? 42.298  77.683  151.811 1.00 45.37 ? 39   ARG A NH1   1 
ATOM   1201  N  NH2   . ARG I  3 39  ? 43.105  77.902  153.954 1.00 49.92 ? 39   ARG A NH2   1 
ATOM   1202  N  N     . SER I  3 40  ? 43.584  81.441  145.711 1.00 23.00 ? 40   SER A N     1 
ATOM   1203  C  CA    . SER I  3 40  ? 44.081  81.862  144.394 1.00 22.32 ? 40   SER A CA    1 
ATOM   1204  C  C     . SER I  3 40  ? 43.767  83.345  144.175 1.00 23.21 ? 40   SER A C     1 
ATOM   1205  O  O     . SER I  3 40  ? 44.630  84.131  143.775 1.00 20.30 ? 40   SER A O     1 
ATOM   1206  C  CB    . SER I  3 40  ? 43.436  81.034  143.277 1.00 18.63 ? 40   SER A CB    1 
ATOM   1207  O  OG    . SER I  3 40  ? 43.935  81.408  141.987 1.00 20.79 ? 40   SER A OG    1 
ATOM   1208  N  N     . PHE I  3 41  ? 42.513  83.711  144.441 1.00 22.96 ? 41   PHE A N     1 
ATOM   1209  C  CA    . PHE I  3 41  ? 42.045  85.091  144.316 1.00 22.41 ? 41   PHE A CA    1 
ATOM   1210  C  C     . PHE I  3 41  ? 42.921  86.054  145.111 1.00 22.21 ? 41   PHE A C     1 
ATOM   1211  O  O     . PHE I  3 41  ? 43.393  87.056  144.575 1.00 20.63 ? 41   PHE A O     1 
ATOM   1212  C  CB    . PHE I  3 41  ? 40.595  85.178  144.833 1.00 24.17 ? 41   PHE A CB    1 
ATOM   1213  C  CG    . PHE I  3 41  ? 40.016  86.568  144.795 1.00 24.03 ? 41   PHE A CG    1 
ATOM   1214  C  CD1   . PHE I  3 41  ? 39.193  86.959  143.743 1.00 23.73 ? 41   PHE A CD1   1 
ATOM   1215  C  CD2   . PHE I  3 41  ? 40.298  87.482  145.813 1.00 29.38 ? 41   PHE A CD2   1 
ATOM   1216  C  CE1   . PHE I  3 41  ? 38.653  88.249  143.701 1.00 26.66 ? 41   PHE A CE1   1 
ATOM   1217  C  CE2   . PHE I  3 41  ? 39.766  88.779  145.777 1.00 29.40 ? 41   PHE A CE2   1 
ATOM   1218  C  CZ    . PHE I  3 41  ? 38.941  89.154  144.718 1.00 25.22 ? 41   PHE A CZ    1 
ATOM   1219  N  N     . ASN I  3 42  ? 43.137  85.753  146.392 1.00 22.57 ? 42   ASN A N     1 
ATOM   1220  C  CA    . ASN I  3 42  ? 43.947  86.624  147.240 1.00 23.01 ? 42   ASN A CA    1 
ATOM   1221  C  C     . ASN I  3 42  ? 45.433  86.653  146.918 1.00 20.56 ? 42   ASN A C     1 
ATOM   1222  O  O     . ASN I  3 42  ? 46.077  87.707  147.019 1.00 21.42 ? 42   ASN A O     1 
ATOM   1223  C  CB    . ASN I  3 42  ? 43.760  86.272  148.719 1.00 25.90 ? 42   ASN A CB    1 
ATOM   1224  C  CG    . ASN I  3 42  ? 42.364  86.574  149.199 1.00 29.67 ? 42   ASN A CG    1 
ATOM   1225  O  OD1   . ASN I  3 42  ? 41.793  87.600  148.833 1.00 27.71 ? 42   ASN A OD1   1 
ATOM   1226  N  ND2   . ASN I  3 42  ? 41.805  85.692  150.017 1.00 32.17 ? 42   ASN A ND2   1 
ATOM   1227  N  N     . ILE I  3 43  ? 45.992  85.503  146.551 1.00 23.09 ? 43   ILE A N     1 
ATOM   1228  C  CA    . ILE I  3 43  ? 47.408  85.462  146.210 1.00 21.08 ? 43   ILE A CA    1 
ATOM   1229  C  C     . ILE I  3 43  ? 47.639  86.290  144.941 1.00 20.50 ? 43   ILE A C     1 
ATOM   1230  O  O     . ILE I  3 43  ? 48.528  87.130  144.899 1.00 22.79 ? 43   ILE A O     1 
ATOM   1231  C  CB    . ILE I  3 43  ? 47.912  84.001  145.989 1.00 22.22 ? 43   ILE A CB    1 
ATOM   1232  C  CG1   . ILE I  3 43  ? 47.911  83.236  147.322 1.00 24.52 ? 43   ILE A CG1   1 
ATOM   1233  C  CG2   . ILE I  3 43  ? 49.341  84.019  145.433 1.00 21.36 ? 43   ILE A CG2   1 
ATOM   1234  C  CD1   . ILE I  3 43  ? 48.152  81.747  147.138 1.00 23.33 ? 43   ILE A CD1   1 
ATOM   1235  N  N     . ALA I  3 44  ? 46.823  86.068  143.920 1.00 20.65 ? 44   ALA A N     1 
ATOM   1236  C  CA    . ALA I  3 44  ? 46.971  86.802  142.665 1.00 23.96 ? 44   ALA A CA    1 
ATOM   1237  C  C     . ALA I  3 44  ? 46.826  88.319  142.846 1.00 23.72 ? 44   ALA A C     1 
ATOM   1238  O  O     . ALA I  3 44  ? 47.531  89.108  142.215 1.00 24.25 ? 44   ALA A O     1 
ATOM   1239  C  CB    . ALA I  3 44  ? 45.974  86.316  141.675 1.00 19.41 ? 44   ALA A CB    1 
ATOM   1240  N  N     . LYS I  3 45  ? 45.892  88.713  143.698 1.00 24.08 ? 45   LYS A N     1 
ATOM   1241  C  CA    . LYS I  3 45  ? 45.664  90.126  143.973 1.00 25.66 ? 45   LYS A CA    1 
ATOM   1242  C  C     . LYS I  3 45  ? 46.883  90.733  144.659 1.00 22.70 ? 45   LYS A C     1 
ATOM   1243  O  O     . LYS I  3 45  ? 47.312  91.843  144.316 1.00 23.29 ? 45   LYS A O     1 
ATOM   1244  C  CB    . LYS I  3 45  ? 44.456  90.275  144.886 1.00 29.12 ? 45   LYS A CB    1 
ATOM   1245  C  CG    . LYS I  3 45  ? 43.949  91.686  144.997 1.00 35.90 ? 45   LYS A CG    1 
ATOM   1246  C  CD    . LYS I  3 45  ? 42.875  91.909  143.963 1.00 41.05 ? 45   LYS A CD    1 
ATOM   1247  C  CE    . LYS I  3 45  ? 41.957  93.044  144.371 1.00 40.99 ? 45   LYS A CE    1 
ATOM   1248  N  NZ    . LYS I  3 45  ? 40.785  93.099  143.470 1.00 40.29 ? 45   LYS A NZ    1 
ATOM   1249  N  N     . GLY I  3 46  ? 47.416  90.010  145.645 1.00 19.80 ? 46   GLY A N     1 
ATOM   1250  C  CA    . GLY I  3 46  ? 48.593  90.489  146.348 1.00 22.48 ? 46   GLY A CA    1 
ATOM   1251  C  C     . GLY I  3 46  ? 49.771  90.655  145.389 1.00 21.49 ? 46   GLY A C     1 
ATOM   1252  O  O     . GLY I  3 46  ? 50.507  91.650  145.436 1.00 21.79 ? 46   GLY A O     1 
ATOM   1253  N  N     . ILE I  3 47  ? 49.960  89.677  144.509 1.00 22.83 ? 47   ILE A N     1 
ATOM   1254  C  CA    . ILE I  3 47  ? 51.067  89.764  143.566 1.00 22.20 ? 47   ILE A CA    1 
ATOM   1255  C  C     . ILE I  3 47  ? 50.900  90.960  142.624 1.00 20.36 ? 47   ILE A C     1 
ATOM   1256  O  O     . ILE I  3 47  ? 51.842  91.735  142.417 1.00 21.27 ? 47   ILE A O     1 
ATOM   1257  C  CB    . ILE I  3 47  ? 51.187  88.461  142.731 1.00 20.07 ? 47   ILE A CB    1 
ATOM   1258  C  CG1   . ILE I  3 47  ? 51.696  87.325  143.614 1.00 20.76 ? 47   ILE A CG1   1 
ATOM   1259  C  CG2   . ILE I  3 47  ? 52.133  88.681  141.556 1.00 21.06 ? 47   ILE A CG2   1 
ATOM   1260  C  CD1   . ILE I  3 47  ? 51.765  85.966  142.883 1.00 21.44 ? 47   ILE A CD1   1 
ATOM   1261  N  N     . ALA I  3 48  ? 49.694  91.126  142.079 1.00 21.52 ? 48   ALA A N     1 
ATOM   1262  C  CA    . ALA I  3 48  ? 49.437  92.235  141.163 1.00 23.42 ? 48   ALA A CA    1 
ATOM   1263  C  C     . ALA I  3 48  ? 49.670  93.569  141.879 1.00 24.37 ? 48   ALA A C     1 
ATOM   1264  O  O     . ALA I  3 48  ? 50.171  94.521  141.283 1.00 23.51 ? 48   ALA A O     1 
ATOM   1265  C  CB    . ALA I  3 48  ? 48.018  92.154  140.623 1.00 24.55 ? 48   ALA A CB    1 
ATOM   1266  N  N     . ASP I  3 49  ? 49.324  93.649  143.162 1.00 23.60 ? 49   ASP A N     1 
ATOM   1267  C  CA    . ASP I  3 49  ? 49.553  94.903  143.895 1.00 26.44 ? 49   ASP A CA    1 
ATOM   1268  C  C     . ASP I  3 49  ? 51.059  95.166  143.994 1.00 25.03 ? 49   ASP A C     1 
ATOM   1269  O  O     . ASP I  3 49  ? 51.530  96.284  143.789 1.00 26.07 ? 49   ASP A O     1 
ATOM   1270  C  CB    . ASP I  3 49  ? 48.957  94.840  145.309 1.00 29.10 ? 49   ASP A CB    1 
ATOM   1271  C  CG    . ASP I  3 49  ? 49.134  96.152  146.073 1.00 40.20 ? 49   ASP A CG    1 
ATOM   1272  O  OD1   . ASP I  3 49  ? 48.521  97.167  145.664 1.00 43.45 ? 49   ASP A OD1   1 
ATOM   1273  O  OD2   . ASP I  3 49  ? 49.898  96.177  147.069 1.00 40.42 ? 49   ASP A OD2   1 
ATOM   1274  N  N     . LEU I  3 50  ? 51.817  94.121  144.300 1.00 21.77 ? 50   LEU A N     1 
ATOM   1275  C  CA    . LEU I  3 50  ? 53.254  94.255  144.409 1.00 23.57 ? 50   LEU A CA    1 
ATOM   1276  C  C     . LEU I  3 50  ? 53.894  94.590  143.064 1.00 23.36 ? 50   LEU A C     1 
ATOM   1277  O  O     . LEU I  3 50  ? 55.023  95.084  143.012 1.00 25.18 ? 50   LEU A O     1 
ATOM   1278  C  CB    . LEU I  3 50  ? 53.845  92.973  144.985 1.00 24.55 ? 50   LEU A CB    1 
ATOM   1279  C  CG    . LEU I  3 50  ? 53.554  92.820  146.482 1.00 22.84 ? 50   LEU A CG    1 
ATOM   1280  C  CD1   . LEU I  3 50  ? 54.130  91.494  146.952 1.00 21.67 ? 50   LEU A CD1   1 
ATOM   1281  C  CD2   . LEU I  3 50  ? 54.159  93.994  147.265 1.00 23.28 ? 50   LEU A CD2   1 
ATOM   1282  N  N     . LEU I  3 51  ? 53.161  94.338  141.982 1.00 23.59 ? 51   LEU A N     1 
ATOM   1283  C  CA    . LEU I  3 51  ? 53.646  94.631  140.633 1.00 22.94 ? 51   LEU A CA    1 
ATOM   1284  C  C     . LEU I  3 51  ? 53.128  95.986  140.149 1.00 26.83 ? 51   LEU A C     1 
ATOM   1285  O  O     . LEU I  3 51  ? 53.399  96.405  139.020 1.00 26.77 ? 51   LEU A O     1 
ATOM   1286  C  CB    . LEU I  3 51  ? 53.198  93.524  139.680 1.00 21.40 ? 51   LEU A CB    1 
ATOM   1287  C  CG    . LEU I  3 51  ? 54.204  92.386  139.452 1.00 27.27 ? 51   LEU A CG    1 
ATOM   1288  C  CD1   . LEU I  3 51  ? 54.585  91.716  140.753 1.00 30.95 ? 51   LEU A CD1   1 
ATOM   1289  C  CD2   . LEU I  3 51  ? 53.599  91.379  138.496 1.00 25.98 ? 51   LEU A CD2   1 
ATOM   1290  N  N     . HIS I  3 52  ? 52.380  96.655  141.023 1.00 29.51 ? 52   HIS A N     1 
ATOM   1291  C  CA    . HIS I  3 52  ? 51.788  97.961  140.747 1.00 29.88 ? 52   HIS A CA    1 
ATOM   1292  C  C     . HIS I  3 52  ? 50.762  97.958  139.617 1.00 30.09 ? 52   HIS A C     1 
ATOM   1293  O  O     . HIS I  3 52  ? 50.641  98.930  138.859 1.00 30.45 ? 52   HIS A O     1 
ATOM   1294  C  CB    . HIS I  3 52  ? 52.885  98.990  140.456 1.00 35.15 ? 52   HIS A CB    1 
ATOM   1295  C  CG    . HIS I  3 52  ? 53.950  99.040  141.505 1.00 42.53 ? 52   HIS A CG    1 
ATOM   1296  N  ND1   . HIS I  3 52  ? 53.693  99.400  142.812 1.00 44.92 ? 52   HIS A ND1   1 
ATOM   1297  C  CD2   . HIS I  3 52  ? 55.275  98.766  141.444 1.00 45.08 ? 52   HIS A CD2   1 
ATOM   1298  C  CE1   . HIS I  3 52  ? 54.814  99.346  143.509 1.00 46.83 ? 52   HIS A CE1   1 
ATOM   1299  N  NE2   . HIS I  3 52  ? 55.790  98.963  142.704 1.00 47.26 ? 52   HIS A NE2   1 
ATOM   1300  N  N     . SER I  3 53  ? 50.013  96.865  139.498 1.00 27.96 ? 53   SER A N     1 
ATOM   1301  C  CA    . SER I  3 53  ? 48.985  96.769  138.473 1.00 28.04 ? 53   SER A CA    1 
ATOM   1302  C  C     . SER I  3 53  ? 47.855  97.699  138.887 1.00 30.31 ? 53   SER A C     1 
ATOM   1303  O  O     . SER I  3 53  ? 47.433  97.674  140.046 1.00 31.18 ? 53   SER A O     1 
ATOM   1304  C  CB    . SER I  3 53  ? 48.435  95.347  138.381 1.00 24.64 ? 53   SER A CB    1 
ATOM   1305  O  OG    . SER I  3 53  ? 47.424  95.252  137.388 1.00 25.18 ? 53   SER A OG    1 
ATOM   1306  N  N     . GLU I  3 54  ? 47.353  98.495  137.951 1.00 29.33 ? 54   GLU A N     1 
ATOM   1307  C  CA    . GLU I  3 54  ? 46.265  99.428  138.280 1.00 35.37 ? 54   GLU A CA    1 
ATOM   1308  C  C     . GLU I  3 54  ? 45.106  99.349  137.298 1.00 32.36 ? 54   GLU A C     1 
ATOM   1309  O  O     . GLU I  3 54  ? 43.980  99.757  137.591 1.00 31.85 ? 54   GLU A O     1 
ATOM   1310  C  CB    . GLU I  3 54  ? 46.807  100.870 138.325 1.00 39.64 ? 54   GLU A CB    1 
ATOM   1311  C  CG    . GLU I  3 54  ? 47.786  101.116 139.463 1.00 49.48 ? 54   GLU A CG    1 
ATOM   1312  C  CD    . GLU I  3 54  ? 48.328  102.542 139.506 1.00 55.28 ? 54   GLU A CD    1 
ATOM   1313  O  OE1   . GLU I  3 54  ? 47.846  103.404 138.733 1.00 56.84 ? 54   GLU A OE1   1 
ATOM   1314  O  OE2   . GLU I  3 54  ? 49.241  102.794 140.328 1.00 58.23 ? 54   GLU A OE2   1 
ATOM   1315  N  N     . THR I  3 55  ? 45.382  98.799  136.129 1.00 29.60 ? 55   THR A N     1 
ATOM   1316  C  CA    . THR I  3 55  ? 44.379  98.709  135.086 1.00 26.62 ? 55   THR A CA    1 
ATOM   1317  C  C     . THR I  3 55  ? 43.204  97.779  135.381 1.00 27.83 ? 55   THR A C     1 
ATOM   1318  O  O     . THR I  3 55  ? 43.372  96.683  135.930 1.00 27.40 ? 55   THR A O     1 
ATOM   1319  C  CB    . THR I  3 55  ? 45.023  98.265  133.771 1.00 26.95 ? 55   THR A CB    1 
ATOM   1320  O  OG1   . THR I  3 55  ? 46.023  99.221  133.396 1.00 29.92 ? 55   THR A OG1   1 
ATOM   1321  C  CG2   . THR I  3 55  ? 43.973  98.146  132.667 1.00 29.90 ? 55   THR A CG2   1 
ATOM   1322  N  N     . VAL I  3 56  ? 42.011  98.250  135.041 1.00 23.64 ? 56   VAL A N     1 
ATOM   1323  C  CA    . VAL I  3 56  ? 40.815  97.443  135.204 1.00 22.26 ? 56   VAL A CA    1 
ATOM   1324  C  C     . VAL I  3 56  ? 40.362  97.131  133.799 1.00 22.91 ? 56   VAL A C     1 
ATOM   1325  O  O     . VAL I  3 56  ? 40.132  98.039  132.990 1.00 28.46 ? 56   VAL A O     1 
ATOM   1326  C  CB    . VAL I  3 56  ? 39.662  98.182  135.930 1.00 22.61 ? 56   VAL A CB    1 
ATOM   1327  C  CG1   . VAL I  3 56  ? 38.381  97.318  135.849 1.00 25.54 ? 56   VAL A CG1   1 
ATOM   1328  C  CG2   . VAL I  3 56  ? 40.037  98.427  137.395 1.00 24.23 ? 56   VAL A CG2   1 
ATOM   1329  N  N     . SER I  3 57  ? 40.257  95.849  133.487 1.00 24.52 ? 57   SER A N     1 
ATOM   1330  C  CA    . SER I  3 57  ? 39.804  95.442  132.169 1.00 24.34 ? 57   SER A CA    1 
ATOM   1331  C  C     . SER I  3 57  ? 39.313  94.003  132.244 1.00 25.25 ? 57   SER A C     1 
ATOM   1332  O  O     . SER I  3 57  ? 39.640  93.269  133.184 1.00 22.14 ? 57   SER A O     1 
ATOM   1333  C  CB    . SER I  3 57  ? 40.941  95.560  131.152 1.00 30.60 ? 57   SER A CB    1 
ATOM   1334  O  OG    . SER I  3 57  ? 41.978  94.654  131.469 1.00 36.77 ? 57   SER A OG    1 
ATOM   1335  N  N     . GLU I  3 58  ? 38.503  93.612  131.267 1.00 25.42 ? 58   GLU A N     1 
ATOM   1336  C  CA    . GLU I  3 58  ? 37.984  92.258  131.232 1.00 26.70 ? 58   GLU A CA    1 
ATOM   1337  C  C     . GLU I  3 58  ? 39.126  91.289  130.968 1.00 26.14 ? 58   GLU A C     1 
ATOM   1338  O  O     . GLU I  3 58  ? 40.096  91.627  130.278 1.00 24.83 ? 58   GLU A O     1 
ATOM   1339  C  CB    . GLU I  3 58  ? 36.916  92.111  130.142 1.00 32.62 ? 58   GLU A CB    1 
ATOM   1340  C  CG    . GLU I  3 58  ? 35.537  92.633  130.562 1.00 42.09 ? 58   GLU A CG    1 
ATOM   1341  C  CD    . GLU I  3 58  ? 34.903  91.813  131.692 1.00 47.51 ? 58   GLU A CD    1 
ATOM   1342  O  OE1   . GLU I  3 58  ? 34.502  90.654  131.442 1.00 49.56 ? 58   GLU A OE1   1 
ATOM   1343  O  OE2   . GLU I  3 58  ? 34.807  92.322  132.831 1.00 46.02 ? 58   GLU A OE2   1 
ATOM   1344  N  N     . ARG I  3 59  ? 39.018  90.107  131.566 1.00 23.03 ? 59   ARG A N     1 
ATOM   1345  C  CA    . ARG I  3 59  ? 40.003  89.040  131.412 1.00 23.31 ? 59   ARG A CA    1 
ATOM   1346  C  C     . ARG I  3 59  ? 40.123  88.732  129.912 1.00 20.87 ? 59   ARG A C     1 
ATOM   1347  O  O     . ARG I  3 59  ? 39.126  88.574  129.213 1.00 24.36 ? 59   ARG A O     1 
ATOM   1348  C  CB    . ARG I  3 59  ? 39.516  87.794  132.166 1.00 23.40 ? 59   ARG A CB    1 
ATOM   1349  C  CG    . ARG I  3 59  ? 40.557  86.736  132.414 1.00 27.41 ? 59   ARG A CG    1 
ATOM   1350  C  CD    . ARG I  3 59  ? 39.880  85.501  133.011 1.00 27.22 ? 59   ARG A CD    1 
ATOM   1351  N  NE    . ARG I  3 59  ? 40.855  84.569  133.546 1.00 30.38 ? 59   ARG A NE    1 
ATOM   1352  C  CZ    . ARG I  3 59  ? 41.114  84.407  134.838 1.00 31.98 ? 59   ARG A CZ    1 
ATOM   1353  N  NH1   . ARG I  3 59  ? 40.461  85.115  135.760 1.00 23.58 ? 59   ARG A NH1   1 
ATOM   1354  N  NH2   . ARG I  3 59  ? 42.045  83.538  135.206 1.00 29.43 ? 59   ARG A NH2   1 
ATOM   1355  N  N     . LEU I  3 60  ? 41.350  88.650  129.414 1.00 23.43 ? 60   LEU A N     1 
ATOM   1356  C  CA    . LEU I  3 60  ? 41.517  88.349  127.997 1.00 23.19 ? 60   LEU A CA    1 
ATOM   1357  C  C     . LEU I  3 60  ? 41.211  86.885  127.735 1.00 21.25 ? 60   LEU A C     1 
ATOM   1358  O  O     . LEU I  3 60  ? 41.277  86.046  128.634 1.00 22.13 ? 60   LEU A O     1 
ATOM   1359  C  CB    . LEU I  3 60  ? 42.967  88.609  127.554 1.00 23.78 ? 60   LEU A CB    1 
ATOM   1360  C  CG    . LEU I  3 60  ? 43.551  89.998  127.777 1.00 26.14 ? 60   LEU A CG    1 
ATOM   1361  C  CD1   . LEU I  3 60  ? 44.965  90.068  127.165 1.00 27.25 ? 60   LEU A CD1   1 
ATOM   1362  C  CD2   . LEU I  3 60  ? 42.641  91.017  127.148 1.00 27.42 ? 60   LEU A CD2   1 
ATOM   1363  N  N     . PRO I  3 61  ? 40.843  86.563  126.495 1.00 19.53 ? 61   PRO A N     1 
ATOM   1364  C  CA    . PRO I  3 61  ? 40.557  85.176  126.129 1.00 20.09 ? 61   PRO A CA    1 
ATOM   1365  C  C     . PRO I  3 61  ? 41.831  84.390  126.425 1.00 19.65 ? 61   PRO A C     1 
ATOM   1366  O  O     . PRO I  3 61  ? 42.945  84.903  126.220 1.00 19.48 ? 61   PRO A O     1 
ATOM   1367  C  CB    . PRO I  3 61  ? 40.313  85.255  124.626 1.00 20.80 ? 61   PRO A CB    1 
ATOM   1368  C  CG    . PRO I  3 61  ? 39.735  86.622  124.452 1.00 21.48 ? 61   PRO A CG    1 
ATOM   1369  C  CD    . PRO I  3 61  ? 40.588  87.479  125.368 1.00 20.51 ? 61   PRO A CD    1 
ATOM   1370  N  N     . GLY I  3 62  ? 41.683  83.157  126.917 1.00 20.73 ? 62   GLY A N     1 
ATOM   1371  C  CA    . GLY I  3 62  ? 42.858  82.344  127.222 1.00 20.52 ? 62   GLY A CA    1 
ATOM   1372  C  C     . GLY I  3 62  ? 43.834  82.155  126.071 1.00 20.35 ? 62   GLY A C     1 
ATOM   1373  O  O     . GLY I  3 62  ? 45.028  82.025  126.292 1.00 22.11 ? 62   GLY A O     1 
ATOM   1374  N  N     . GLN I  3 63  ? 43.347  82.099  124.843 1.00 19.56 ? 63   GLN A N     1 
ATOM   1375  C  CA    . GLN I  3 63  ? 44.254  81.952  123.691 1.00 18.53 ? 63   GLN A CA    1 
ATOM   1376  C  C     . GLN I  3 63  ? 45.147  83.198  123.555 1.00 22.33 ? 63   GLN A C     1 
ATOM   1377  O  O     . GLN I  3 63  ? 46.310  83.121  123.155 1.00 18.83 ? 63   GLN A O     1 
ATOM   1378  C  CB    . GLN I  3 63  ? 43.441  81.779  122.412 1.00 19.71 ? 63   GLN A CB    1 
ATOM   1379  C  CG    . GLN I  3 63  ? 42.469  80.608  122.444 1.00 19.92 ? 63   GLN A CG    1 
ATOM   1380  C  CD    . GLN I  3 63  ? 41.091  80.954  122.979 1.00 17.79 ? 63   GLN A CD    1 
ATOM   1381  O  OE1   . GLN I  3 63  ? 40.899  81.963  123.683 1.00 20.80 ? 63   GLN A OE1   1 
ATOM   1382  N  NE2   . GLN I  3 63  ? 40.124  80.104  122.675 1.00 18.19 ? 63   GLN A NE2   1 
ATOM   1383  N  N     . THR I  3 64  ? 44.589  84.355  123.884 1.00 19.73 ? 64   THR A N     1 
ATOM   1384  C  CA    . THR I  3 64  ? 45.329  85.602  123.809 1.00 17.63 ? 64   THR A CA    1 
ATOM   1385  C  C     . THR I  3 64  ? 46.398  85.691  124.906 1.00 20.01 ? 64   THR A C     1 
ATOM   1386  O  O     . THR I  3 64  ? 47.567  86.023  124.648 1.00 21.05 ? 64   THR A O     1 
ATOM   1387  C  CB    . THR I  3 64  ? 44.372  86.789  123.957 1.00 19.64 ? 64   THR A CB    1 
ATOM   1388  O  OG1   . THR I  3 64  ? 43.350  86.693  122.956 1.00 20.77 ? 64   THR A OG1   1 
ATOM   1389  C  CG2   . THR I  3 64  ? 45.126  88.103  123.781 1.00 22.53 ? 64   THR A CG2   1 
ATOM   1390  N  N     . SER I  3 65  ? 46.018  85.396  126.144 1.00 18.98 ? 65   SER A N     1 
ATOM   1391  C  CA    . SER I  3 65  ? 47.004  85.468  127.210 1.00 18.47 ? 65   SER A CA    1 
ATOM   1392  C  C     . SER I  3 65  ? 48.080  84.383  127.041 1.00 18.12 ? 65   SER A C     1 
ATOM   1393  O  O     . SER I  3 65  ? 49.262  84.635  127.347 1.00 17.90 ? 65   SER A O     1 
ATOM   1394  C  CB    . SER I  3 65  ? 46.336  85.333  128.591 1.00 18.83 ? 65   SER A CB    1 
ATOM   1395  O  OG    . SER I  3 65  ? 45.502  84.173  128.642 1.00 22.86 ? 65   SER A OG    1 
ATOM   1396  N  N     . GLY I  3 66  ? 47.663  83.210  126.567 1.00 17.25 ? 66   GLY A N     1 
ATOM   1397  C  CA    . GLY I  3 66  ? 48.596  82.107  126.349 1.00 15.96 ? 66   GLY A CA    1 
ATOM   1398  C  C     . GLY I  3 66  ? 49.668  82.532  125.363 1.00 17.37 ? 66   GLY A C     1 
ATOM   1399  O  O     . GLY I  3 66  ? 50.864  82.432  125.619 1.00 17.85 ? 66   GLY A O     1 
ATOM   1400  N  N     . ASN I  3 67  ? 49.225  83.035  124.213 1.00 16.94 ? 67   ASN A N     1 
ATOM   1401  C  CA    . ASN I  3 67  ? 50.172  83.476  123.179 1.00 18.47 ? 67   ASN A CA    1 
ATOM   1402  C  C     . ASN I  3 67  ? 51.032  84.674  123.603 1.00 19.82 ? 67   ASN A C     1 
ATOM   1403  O  O     . ASN I  3 67  ? 52.253  84.705  123.380 1.00 19.43 ? 67   ASN A O     1 
ATOM   1404  C  CB    . ASN I  3 67  ? 49.389  83.812  121.901 1.00 18.01 ? 67   ASN A CB    1 
ATOM   1405  C  CG    . ASN I  3 67  ? 50.279  84.345  120.797 1.00 22.98 ? 67   ASN A CG    1 
ATOM   1406  O  OD1   . ASN I  3 67  ? 50.191  85.520  120.434 1.00 30.12 ? 67   ASN A OD1   1 
ATOM   1407  N  ND2   . ASN I  3 67  ? 51.146  83.488  120.267 1.00 24.12 ? 67   ASN A ND2   1 
ATOM   1408  N  N     . ALA I  3 68  ? 50.406  85.669  124.230 1.00 18.93 ? 68   ALA A N     1 
ATOM   1409  C  CA    . ALA I  3 68  ? 51.133  86.854  124.652 1.00 19.19 ? 68   ALA A CA    1 
ATOM   1410  C  C     . ALA I  3 68  ? 52.165  86.526  125.713 1.00 19.07 ? 68   ALA A C     1 
ATOM   1411  O  O     . ALA I  3 68  ? 53.256  87.090  125.717 1.00 17.62 ? 68   ALA A O     1 
ATOM   1412  C  CB    . ALA I  3 68  ? 50.145  87.943  125.160 1.00 19.91 ? 68   ALA A CB    1 
ATOM   1413  N  N     . PHE I  3 69  ? 51.837  85.597  126.610 1.00 18.75 ? 69   PHE A N     1 
ATOM   1414  C  CA    . PHE I  3 69  ? 52.768  85.226  127.671 1.00 19.43 ? 69   PHE A CA    1 
ATOM   1415  C  C     . PHE I  3 69  ? 54.000  84.566  127.034 1.00 17.81 ? 69   PHE A C     1 
ATOM   1416  O  O     . PHE I  3 69  ? 55.123  84.815  127.459 1.00 18.74 ? 69   PHE A O     1 
ATOM   1417  C  CB    . PHE I  3 69  ? 52.082  84.276  128.687 1.00 18.63 ? 69   PHE A CB    1 
ATOM   1418  C  CG    . PHE I  3 69  ? 52.939  83.939  129.896 1.00 17.91 ? 69   PHE A CG    1 
ATOM   1419  C  CD1   . PHE I  3 69  ? 53.449  84.944  130.725 1.00 17.20 ? 69   PHE A CD1   1 
ATOM   1420  C  CD2   . PHE I  3 69  ? 53.219  82.600  130.206 1.00 19.51 ? 69   PHE A CD2   1 
ATOM   1421  C  CE1   . PHE I  3 69  ? 54.218  84.635  131.838 1.00 16.58 ? 69   PHE A CE1   1 
ATOM   1422  C  CE2   . PHE I  3 69  ? 53.996  82.280  131.338 1.00 17.83 ? 69   PHE A CE2   1 
ATOM   1423  C  CZ    . PHE I  3 69  ? 54.495  83.300  132.153 1.00 15.59 ? 69   PHE A CZ    1 
ATOM   1424  N  N     . GLU I  3 70  ? 53.783  83.736  126.013 1.00 16.23 ? 70   GLU A N     1 
ATOM   1425  C  CA    . GLU I  3 70  ? 54.905  83.095  125.342 1.00 17.27 ? 70   GLU A CA    1 
ATOM   1426  C  C     . GLU I  3 70  ? 55.798  84.168  124.724 1.00 15.06 ? 70   GLU A C     1 
ATOM   1427  O  O     . GLU I  3 70  ? 57.014  84.141  124.866 1.00 16.55 ? 70   GLU A O     1 
ATOM   1428  C  CB    . GLU I  3 70  ? 54.438  82.162  124.215 1.00 17.93 ? 70   GLU A CB    1 
ATOM   1429  C  CG    . GLU I  3 70  ? 53.761  80.880  124.662 1.00 20.78 ? 70   GLU A CG    1 
ATOM   1430  C  CD    . GLU I  3 70  ? 53.267  80.036  123.495 1.00 22.91 ? 70   GLU A CD    1 
ATOM   1431  O  OE1   . GLU I  3 70  ? 53.531  80.411  122.327 1.00 22.63 ? 70   GLU A OE1   1 
ATOM   1432  O  OE2   . GLU I  3 70  ? 52.623  78.989  123.745 1.00 22.46 ? 70   GLU A OE2   1 
ATOM   1433  N  N     . ALA I  3 71  ? 55.179  85.110  124.015 1.00 17.30 ? 71   ALA A N     1 
ATOM   1434  C  CA    . ALA I  3 71  ? 55.955  86.151  123.346 1.00 16.51 ? 71   ALA A CA    1 
ATOM   1435  C  C     . ALA I  3 71  ? 56.776  87.003  124.317 1.00 17.22 ? 71   ALA A C     1 
ATOM   1436  O  O     . ALA I  3 71  ? 57.958  87.259  124.096 1.00 16.17 ? 71   ALA A O     1 
ATOM   1437  C  CB    . ALA I  3 71  ? 55.021  87.045  122.519 1.00 18.72 ? 71   ALA A CB    1 
ATOM   1438  N  N     . ILE I  3 72  ? 56.145  87.433  125.409 1.00 17.66 ? 72   ILE A N     1 
ATOM   1439  C  CA    . ILE I  3 72  ? 56.821  88.257  126.399 1.00 17.77 ? 72   ILE A CA    1 
ATOM   1440  C  C     . ILE I  3 72  ? 57.935  87.475  127.117 1.00 17.93 ? 72   ILE A C     1 
ATOM   1441  O  O     . ILE I  3 72  ? 58.993  88.028  127.408 1.00 19.10 ? 72   ILE A O     1 
ATOM   1442  C  CB    . ILE I  3 72  ? 55.772  88.838  127.365 1.00 16.94 ? 72   ILE A CB    1 
ATOM   1443  C  CG1   . ILE I  3 72  ? 54.918  89.838  126.564 1.00 20.76 ? 72   ILE A CG1   1 
ATOM   1444  C  CG2   . ILE I  3 72  ? 56.433  89.497  128.545 1.00 22.41 ? 72   ILE A CG2   1 
ATOM   1445  C  CD1   . ILE I  3 72  ? 53.641  90.322  127.262 1.00 20.41 ? 72   ILE A CD1   1 
ATOM   1446  N  N     . CYS I  3 73  ? 57.692  86.192  127.397 1.00 17.40 ? 73   CYS A N     1 
ATOM   1447  C  CA    . CYS I  3 73  ? 58.729  85.363  128.008 1.00 16.37 ? 73   CYS A CA    1 
ATOM   1448  C  C     . CYS I  3 73  ? 59.921  85.255  127.057 1.00 17.91 ? 73   CYS A C     1 
ATOM   1449  O  O     . CYS I  3 73  ? 61.081  85.356  127.488 1.00 17.63 ? 73   CYS A O     1 
ATOM   1450  C  CB    . CYS I  3 73  ? 58.185  83.959  128.306 1.00 18.91 ? 73   CYS A CB    1 
ATOM   1451  S  SG    . CYS I  3 73  ? 57.232  83.869  129.867 1.00 19.42 ? 73   CYS A SG    1 
ATOM   1452  N  N     . SER I  3 74  ? 59.631  85.077  125.766 1.00 17.41 ? 74   SER A N     1 
ATOM   1453  C  CA    . SER I  3 74  ? 60.680  84.961  124.753 1.00 20.46 ? 74   SER A CA    1 
ATOM   1454  C  C     . SER I  3 74  ? 61.567  86.200  124.700 1.00 21.50 ? 74   SER A C     1 
ATOM   1455  O  O     . SER I  3 74  ? 62.806  86.102  124.630 1.00 17.91 ? 74   SER A O     1 
ATOM   1456  C  CB    . SER I  3 74  ? 60.053  84.749  123.383 1.00 20.60 ? 74   SER A CB    1 
ATOM   1457  O  OG    . SER I  3 74  ? 61.052  84.397  122.442 1.00 32.15 ? 74   SER A OG    1 
ATOM   1458  N  N     . GLU I  3 75  ? 60.934  87.370  124.725 1.00 19.37 ? 75   GLU A N     1 
ATOM   1459  C  CA    . GLU I  3 75  ? 61.668  88.628  124.668 1.00 19.70 ? 75   GLU A CA    1 
ATOM   1460  C  C     . GLU I  3 75  ? 62.562  88.821  125.883 1.00 20.67 ? 75   GLU A C     1 
ATOM   1461  O  O     . GLU I  3 75  ? 63.680  89.293  125.753 1.00 21.25 ? 75   GLU A O     1 
ATOM   1462  C  CB    . GLU I  3 75  ? 60.686  89.799  124.524 1.00 19.74 ? 75   GLU A CB    1 
ATOM   1463  C  CG    . GLU I  3 75  ? 59.945  89.737  123.217 1.00 24.17 ? 75   GLU A CG    1 
ATOM   1464  C  CD    . GLU I  3 75  ? 58.930  90.842  123.053 1.00 34.91 ? 75   GLU A CD    1 
ATOM   1465  O  OE1   . GLU I  3 75  ? 58.634  91.549  124.042 1.00 33.20 ? 75   GLU A OE1   1 
ATOM   1466  O  OE2   . GLU I  3 75  ? 58.421  90.994  121.921 1.00 39.40 ? 75   GLU A OE2   1 
ATOM   1467  N  N     . PHE I  3 76  ? 62.065  88.449  127.062 1.00 18.58 ? 76   PHE A N     1 
ATOM   1468  C  CA    . PHE I  3 76  ? 62.844  88.565  128.279 1.00 19.33 ? 76   PHE A CA    1 
ATOM   1469  C  C     . PHE I  3 76  ? 64.060  87.645  128.198 1.00 21.01 ? 76   PHE A C     1 
ATOM   1470  O  O     . PHE I  3 76  ? 65.166  88.048  128.546 1.00 18.97 ? 76   PHE A O     1 
ATOM   1471  C  CB    . PHE I  3 76  ? 62.004  88.173  129.505 1.00 19.34 ? 76   PHE A CB    1 
ATOM   1472  C  CG    . PHE I  3 76  ? 62.813  87.988  130.744 1.00 21.73 ? 76   PHE A CG    1 
ATOM   1473  C  CD1   . PHE I  3 76  ? 63.277  89.087  131.473 1.00 21.18 ? 76   PHE A CD1   1 
ATOM   1474  C  CD2   . PHE I  3 76  ? 63.194  86.708  131.141 1.00 20.97 ? 76   PHE A CD2   1 
ATOM   1475  C  CE1   . PHE I  3 76  ? 64.118  88.904  132.579 1.00 22.31 ? 76   PHE A CE1   1 
ATOM   1476  C  CE2   . PHE I  3 76  ? 64.028  86.515  132.228 1.00 21.16 ? 76   PHE A CE2   1 
ATOM   1477  C  CZ    . PHE I  3 76  ? 64.495  87.604  132.952 1.00 23.25 ? 76   PHE A CZ    1 
ATOM   1478  N  N     . VAL I  3 77  ? 63.846  86.402  127.755 1.00 19.30 ? 77   VAL A N     1 
ATOM   1479  C  CA    . VAL I  3 77  ? 64.952  85.456  127.671 1.00 18.96 ? 77   VAL A CA    1 
ATOM   1480  C  C     . VAL I  3 77  ? 65.995  85.933  126.667 1.00 20.02 ? 77   VAL A C     1 
ATOM   1481  O  O     . VAL I  3 77  ? 67.197  85.942  126.957 1.00 19.16 ? 77   VAL A O     1 
ATOM   1482  C  CB    . VAL I  3 77  ? 64.457  84.031  127.308 1.00 19.11 ? 77   VAL A CB    1 
ATOM   1483  C  CG1   . VAL I  3 77  ? 65.660  83.120  126.942 1.00 17.69 ? 77   VAL A CG1   1 
ATOM   1484  C  CG2   . VAL I  3 77  ? 63.720  83.427  128.513 1.00 19.95 ? 77   VAL A CG2   1 
ATOM   1485  N  N     . GLN I  3 78  ? 65.531  86.361  125.505 1.00 18.25 ? 78   GLN A N     1 
ATOM   1486  C  CA    . GLN I  3 78  ? 66.440  86.847  124.475 1.00 22.01 ? 78   GLN A CA    1 
ATOM   1487  C  C     . GLN I  3 78  ? 67.303  88.002  124.982 1.00 21.38 ? 78   GLN A C     1 
ATOM   1488  O  O     . GLN I  3 78  ? 68.531  87.986  124.870 1.00 22.31 ? 78   GLN A O     1 
ATOM   1489  C  CB    . GLN I  3 78  ? 65.634  87.301  123.267 1.00 23.81 ? 78   GLN A CB    1 
ATOM   1490  C  CG    . GLN I  3 78  ? 66.473  87.692  122.056 1.00 30.85 ? 78   GLN A CG    1 
ATOM   1491  C  CD    . GLN I  3 78  ? 65.605  88.205  120.914 1.00 38.40 ? 78   GLN A CD    1 
ATOM   1492  O  OE1   . GLN I  3 78  ? 64.837  89.156  121.085 1.00 46.06 ? 78   GLN A OE1   1 
ATOM   1493  N  NE2   . GLN I  3 78  ? 65.717  87.577  119.746 1.00 42.71 ? 78   GLN A NE2   1 
ATOM   1494  N  N     . SER I  3 79  ? 66.658  88.992  125.593 1.00 21.68 ? 79   SER A N     1 
ATOM   1495  C  CA    . SER I  3 79  ? 67.373  90.160  126.078 1.00 22.54 ? 79   SER A CA    1 
ATOM   1496  C  C     . SER I  3 79  ? 68.352  89.888  127.215 1.00 22.79 ? 79   SER A C     1 
ATOM   1497  O  O     . SER I  3 79  ? 69.477  90.398  127.216 1.00 23.83 ? 79   SER A O     1 
ATOM   1498  C  CB    . SER I  3 79  ? 66.348  91.232  126.493 1.00 26.62 ? 79   SER A CB    1 
ATOM   1499  O  OG    . SER I  3 79  ? 66.987  92.483  126.658 1.00 35.44 ? 79   SER A OG    1 
ATOM   1500  N  N     . ALA I  3 80  ? 67.947  89.099  128.205 1.00 20.53 ? 80   ALA A N     1 
ATOM   1501  C  CA    . ALA I  3 80  ? 68.833  88.825  129.324 1.00 19.88 ? 80   ALA A CA    1 
ATOM   1502  C  C     . ALA I  3 80  ? 69.983  87.860  128.964 1.00 19.47 ? 80   ALA A C     1 
ATOM   1503  O  O     . ALA I  3 80  ? 71.131  88.069  129.363 1.00 20.23 ? 80   ALA A O     1 
ATOM   1504  C  CB    . ALA I  3 80  ? 68.020  88.271  130.520 1.00 18.22 ? 80   ALA A CB    1 
ATOM   1505  N  N     . PHE I  3 81  ? 69.675  86.819  128.183 1.00 19.55 ? 81   PHE A N     1 
ATOM   1506  C  CA    . PHE I  3 81  ? 70.697  85.844  127.821 1.00 18.29 ? 81   PHE A CA    1 
ATOM   1507  C  C     . PHE I  3 81  ? 71.787  86.460  126.956 1.00 18.26 ? 81   PHE A C     1 
ATOM   1508  O  O     . PHE I  3 81  ? 72.965  86.058  127.027 1.00 19.70 ? 81   PHE A O     1 
ATOM   1509  C  CB    . PHE I  3 81  ? 70.043  84.649  127.098 1.00 17.05 ? 81   PHE A CB    1 
ATOM   1510  C  CG    . PHE I  3 81  ? 70.969  83.474  126.920 1.00 15.30 ? 81   PHE A CG    1 
ATOM   1511  C  CD1   . PHE I  3 81  ? 71.563  82.857  128.017 1.00 16.34 ? 81   PHE A CD1   1 
ATOM   1512  C  CD2   . PHE I  3 81  ? 71.234  82.980  125.645 1.00 19.52 ? 81   PHE A CD2   1 
ATOM   1513  C  CE1   . PHE I  3 81  ? 72.413  81.758  127.853 1.00 20.91 ? 81   PHE A CE1   1 
ATOM   1514  C  CE2   . PHE I  3 81  ? 72.075  81.885  125.471 1.00 19.92 ? 81   PHE A CE2   1 
ATOM   1515  C  CZ    . PHE I  3 81  ? 72.666  81.272  126.570 1.00 21.32 ? 81   PHE A CZ    1 
ATOM   1516  N  N     . GLU I  3 82  ? 71.390  87.440  126.155 1.00 20.02 ? 82   GLU A N     1 
ATOM   1517  C  CA    . GLU I  3 82  ? 72.327  88.146  125.286 1.00 22.38 ? 82   GLU A CA    1 
ATOM   1518  C  C     . GLU I  3 82  ? 73.467  88.777  126.093 1.00 23.64 ? 82   GLU A C     1 
ATOM   1519  O  O     . GLU I  3 82  ? 74.582  88.934  125.582 1.00 24.00 ? 82   GLU A O     1 
ATOM   1520  C  CB    . GLU I  3 82  ? 71.594  89.225  124.486 1.00 26.57 ? 82   GLU A CB    1 
ATOM   1521  C  CG    . GLU I  3 82  ? 72.486  89.955  123.493 1.00 38.87 ? 82   GLU A CG    1 
ATOM   1522  C  CD    . GLU I  3 82  ? 71.718  90.939  122.619 1.00 49.31 ? 82   GLU A CD    1 
ATOM   1523  O  OE1   . GLU I  3 82  ? 70.553  91.264  122.948 1.00 52.37 ? 82   GLU A OE1   1 
ATOM   1524  O  OE2   . GLU I  3 82  ? 72.287  91.397  121.601 1.00 56.63 ? 82   GLU A OE2   1 
ATOM   1525  N  N     . LYS I  3 83  ? 73.206  89.114  127.361 1.00 23.63 ? 83   LYS A N     1 
ATOM   1526  C  CA    . LYS I  3 83  ? 74.220  89.740  128.211 1.00 22.88 ? 83   LYS A CA    1 
ATOM   1527  C  C     . LYS I  3 83  ? 75.185  88.750  128.863 1.00 21.16 ? 83   LYS A C     1 
ATOM   1528  O  O     . LYS I  3 83  ? 76.109  89.139  129.581 1.00 22.14 ? 83   LYS A O     1 
ATOM   1529  C  CB    . LYS I  3 83  ? 73.531  90.599  129.291 1.00 24.56 ? 83   LYS A CB    1 
ATOM   1530  C  CG    . LYS I  3 83  ? 72.636  91.666  128.671 1.00 27.67 ? 83   LYS A CG    1 
ATOM   1531  C  CD    . LYS I  3 83  ? 71.976  92.567  129.695 1.00 32.93 ? 83   LYS A CD    1 
ATOM   1532  C  CE    . LYS I  3 83  ? 71.176  93.677  128.989 1.00 34.47 ? 83   LYS A CE    1 
ATOM   1533  N  NZ    . LYS I  3 83  ? 72.060  94.543  128.124 1.00 37.40 ? 83   LYS A NZ    1 
ATOM   1534  N  N     . LEU I  3 84  ? 74.996  87.462  128.587 1.00 20.50 ? 84   LEU A N     1 
ATOM   1535  C  CA    . LEU I  3 84  ? 75.848  86.448  129.190 1.00 21.20 ? 84   LEU A CA    1 
ATOM   1536  C  C     . LEU I  3 84  ? 76.843  85.812  128.201 1.00 21.21 ? 84   LEU A C     1 
ATOM   1537  O  O     . LEU I  3 84  ? 77.381  84.733  128.449 1.00 21.71 ? 84   LEU A O     1 
ATOM   1538  C  CB    . LEU I  3 84  ? 74.959  85.372  129.837 1.00 20.19 ? 84   LEU A CB    1 
ATOM   1539  C  CG    . LEU I  3 84  ? 74.072  85.875  130.997 1.00 21.07 ? 84   LEU A CG    1 
ATOM   1540  C  CD1   . LEU I  3 84  ? 73.147  84.758  131.466 1.00 21.53 ? 84   LEU A CD1   1 
ATOM   1541  C  CD2   . LEU I  3 84  ? 74.952  86.371  132.150 1.00 20.50 ? 84   LEU A CD2   1 
ATOM   1542  N  N     . GLN I  3 85  ? 77.105  86.492  127.096 1.00 20.63 ? 85   GLN A N     1 
ATOM   1543  C  CA    . GLN I  3 85  ? 78.029  85.960  126.090 1.00 23.31 ? 85   GLN A CA    1 
ATOM   1544  C  C     . GLN I  3 85  ? 79.432  85.615  126.634 1.00 22.96 ? 85   GLN A C     1 
ATOM   1545  O  O     . GLN I  3 85  ? 80.109  84.740  126.091 1.00 25.08 ? 85   GLN A O     1 
ATOM   1546  C  CB    . GLN I  3 85  ? 78.138  86.940  124.917 1.00 25.15 ? 85   GLN A CB    1 
ATOM   1547  C  CG    . GLN I  3 85  ? 79.138  86.511  123.854 1.00 33.19 ? 85   GLN A CG    1 
ATOM   1548  C  CD    . GLN I  3 85  ? 78.531  85.593  122.793 1.00 34.35 ? 85   GLN A CD    1 
ATOM   1549  O  OE1   . GLN I  3 85  ? 79.253  85.015  121.977 1.00 35.69 ? 85   GLN A OE1   1 
ATOM   1550  N  NE2   . GLN I  3 85  ? 77.204  85.475  122.791 1.00 35.34 ? 85   GLN A NE2   1 
ATOM   1551  N  N     . HIS I  3 86  ? 79.884  86.291  127.686 1.00 24.16 ? 86   HIS A N     1 
ATOM   1552  C  CA    . HIS I  3 86  ? 81.203  85.994  128.251 1.00 22.19 ? 86   HIS A CA    1 
ATOM   1553  C  C     . HIS I  3 86  ? 81.232  84.722  129.090 1.00 23.60 ? 86   HIS A C     1 
ATOM   1554  O  O     . HIS I  3 86  ? 82.302  84.158  129.321 1.00 25.53 ? 86   HIS A O     1 
ATOM   1555  C  CB    . HIS I  3 86  ? 81.728  87.179  129.090 1.00 23.51 ? 86   HIS A CB    1 
ATOM   1556  C  CG    . HIS I  3 86  ? 80.864  87.529  130.258 1.00 22.40 ? 86   HIS A CG    1 
ATOM   1557  N  ND1   . HIS I  3 86  ? 79.548  87.914  130.116 1.00 25.53 ? 86   HIS A ND1   1 
ATOM   1558  C  CD2   . HIS I  3 86  ? 81.125  87.553  131.587 1.00 24.05 ? 86   HIS A CD2   1 
ATOM   1559  C  CE1   . HIS I  3 86  ? 79.033  88.160  131.307 1.00 26.79 ? 86   HIS A CE1   1 
ATOM   1560  N  NE2   . HIS I  3 86  ? 79.968  87.950  132.217 1.00 25.58 ? 86   HIS A NE2   1 
ATOM   1561  N  N     . ILE I  3 87  ? 80.079  84.269  129.576 1.00 20.91 ? 87   ILE A N     1 
ATOM   1562  C  CA    . ILE I  3 87  ? 80.086  83.031  130.340 1.00 23.74 ? 87   ILE A CA    1 
ATOM   1563  C  C     . ILE I  3 87  ? 79.505  81.870  129.525 1.00 18.53 ? 87   ILE A C     1 
ATOM   1564  O  O     . ILE I  3 87  ? 79.666  80.707  129.902 1.00 20.61 ? 87   ILE A O     1 
ATOM   1565  C  CB    . ILE I  3 87  ? 79.335  83.140  131.687 1.00 29.45 ? 87   ILE A CB    1 
ATOM   1566  C  CG1   . ILE I  3 87  ? 77.876  83.492  131.453 1.00 26.25 ? 87   ILE A CG1   1 
ATOM   1567  C  CG2   . ILE I  3 87  ? 80.044  84.172  132.603 1.00 28.23 ? 87   ILE A CG2   1 
ATOM   1568  C  CD1   . ILE I  3 87  ? 77.046  83.453  132.743 1.00 30.88 ? 87   ILE A CD1   1 
ATOM   1569  N  N     . ARG I  3 88  ? 78.841  82.190  128.409 1.00 18.53 ? 88   ARG A N     1 
ATOM   1570  C  CA    . ARG I  3 88  ? 78.259  81.171  127.521 1.00 16.79 ? 88   ARG A CA    1 
ATOM   1571  C  C     . ARG I  3 88  ? 78.190  81.743  126.100 1.00 17.46 ? 88   ARG A C     1 
ATOM   1572  O  O     . ARG I  3 88  ? 77.130  82.084  125.569 1.00 17.52 ? 88   ARG A O     1 
ATOM   1573  C  CB    . ARG I  3 88  ? 76.856  80.756  128.000 1.00 18.76 ? 88   ARG A CB    1 
ATOM   1574  C  CG    . ARG I  3 88  ? 76.373  79.396  127.424 1.00 20.27 ? 88   ARG A CG    1 
ATOM   1575  C  CD    . ARG I  3 88  ? 77.230  78.200  127.891 1.00 17.24 ? 88   ARG A CD    1 
ATOM   1576  N  NE    . ARG I  3 88  ? 76.517  76.921  127.745 1.00 16.68 ? 88   ARG A NE    1 
ATOM   1577  C  CZ    . ARG I  3 88  ? 76.455  76.184  126.629 1.00 17.73 ? 88   ARG A CZ    1 
ATOM   1578  N  NH1   . ARG I  3 88  ? 77.082  76.582  125.516 1.00 17.50 ? 88   ARG A NH1   1 
ATOM   1579  N  NH2   . ARG I  3 88  ? 75.744  75.061  126.620 1.00 17.14 ? 88   ARG A NH2   1 
ATOM   1580  N  N     . PRO I  3 89  ? 79.352  81.857  125.467 1.00 18.45 ? 89   PRO A N     1 
ATOM   1581  C  CA    . PRO I  3 89  ? 79.446  82.391  124.113 1.00 18.28 ? 89   PRO A CA    1 
ATOM   1582  C  C     . PRO I  3 89  ? 78.746  81.556  123.050 1.00 20.13 ? 89   PRO A C     1 
ATOM   1583  O  O     . PRO I  3 89  ? 78.545  80.349  123.222 1.00 20.54 ? 89   PRO A O     1 
ATOM   1584  C  CB    . PRO I  3 89  ? 80.957  82.489  123.887 1.00 19.46 ? 89   PRO A CB    1 
ATOM   1585  C  CG    . PRO I  3 89  ? 81.527  81.449  124.765 1.00 18.35 ? 89   PRO A CG    1 
ATOM   1586  C  CD    . PRO I  3 89  ? 80.684  81.550  126.020 1.00 18.55 ? 89   PRO A CD    1 
ATOM   1587  N  N     . GLY I  3 90  ? 78.348  82.212  121.958 1.00 18.26 ? 90   GLY A N     1 
ATOM   1588  C  CA    . GLY I  3 90  ? 77.701  81.487  120.874 1.00 17.62 ? 90   GLY A CA    1 
ATOM   1589  C  C     . GLY I  3 90  ? 76.840  82.401  120.032 1.00 18.56 ? 90   GLY A C     1 
ATOM   1590  O  O     . GLY I  3 90  ? 76.583  83.544  120.426 1.00 19.08 ? 90   GLY A O     1 
ATOM   1591  N  N     . ASP I  3 91  ? 76.398  81.906  118.878 1.00 18.09 ? 91   ASP A N     1 
ATOM   1592  C  CA    . ASP I  3 91  ? 75.527  82.653  117.980 1.00 19.51 ? 91   ASP A CA    1 
ATOM   1593  C  C     . ASP I  3 91  ? 74.153  82.082  118.335 1.00 17.75 ? 91   ASP A C     1 
ATOM   1594  O  O     . ASP I  3 91  ? 73.723  81.089  117.767 1.00 17.77 ? 91   ASP A O     1 
ATOM   1595  C  CB    . ASP I  3 91  ? 75.907  82.318  116.528 1.00 22.11 ? 91   ASP A CB    1 
ATOM   1596  C  CG    . ASP I  3 91  ? 75.039  83.039  115.513 1.00 27.16 ? 91   ASP A CG    1 
ATOM   1597  O  OD1   . ASP I  3 91  ? 74.175  83.845  115.915 1.00 28.13 ? 91   ASP A OD1   1 
ATOM   1598  O  OD2   . ASP I  3 91  ? 75.231  82.793  114.303 1.00 32.10 ? 91   ASP A OD2   1 
ATOM   1599  N  N     . TRP I  3 92  ? 73.480  82.725  119.294 1.00 17.70 ? 92   TRP A N     1 
ATOM   1600  C  CA    . TRP I  3 92  ? 72.197  82.226  119.808 1.00 17.87 ? 92   TRP A CA    1 
ATOM   1601  C  C     . TRP I  3 92  ? 70.951  82.842  119.207 1.00 18.52 ? 92   TRP A C     1 
ATOM   1602  O  O     . TRP I  3 92  ? 70.947  84.017  118.860 1.00 23.24 ? 92   TRP A O     1 
ATOM   1603  C  CB    . TRP I  3 92  ? 72.137  82.447  121.329 1.00 18.40 ? 92   TRP A CB    1 
ATOM   1604  C  CG    . TRP I  3 92  ? 73.317  81.929  122.098 1.00 18.64 ? 92   TRP A CG    1 
ATOM   1605  C  CD1   . TRP I  3 92  ? 74.391  82.649  122.539 1.00 18.54 ? 92   TRP A CD1   1 
ATOM   1606  C  CD2   . TRP I  3 92  ? 73.542  80.573  122.511 1.00 19.23 ? 92   TRP A CD2   1 
ATOM   1607  N  NE1   . TRP I  3 92  ? 75.272  81.824  123.208 1.00 19.58 ? 92   TRP A NE1   1 
ATOM   1608  C  CE2   . TRP I  3 92  ? 74.781  80.546  123.201 1.00 16.59 ? 92   TRP A CE2   1 
ATOM   1609  C  CE3   . TRP I  3 92  ? 72.816  79.378  122.366 1.00 17.95 ? 92   TRP A CE3   1 
ATOM   1610  C  CZ2   . TRP I  3 92  ? 75.317  79.371  123.744 1.00 16.99 ? 92   TRP A CZ2   1 
ATOM   1611  C  CZ3   . TRP I  3 92  ? 73.346  78.207  122.911 1.00 17.36 ? 92   TRP A CZ3   1 
ATOM   1612  C  CH2   . TRP I  3 92  ? 74.587  78.212  123.590 1.00 19.39 ? 92   TRP A CH2   1 
ATOM   1613  N  N     . ASN I  3 93  ? 69.898  82.037  119.080 1.00 15.14 ? 93   ASN A N     1 
ATOM   1614  C  CA    . ASN I  3 93  ? 68.628  82.536  118.581 1.00 19.42 ? 93   ASN A CA    1 
ATOM   1615  C  C     . ASN I  3 93  ? 67.572  82.115  119.581 1.00 20.52 ? 93   ASN A C     1 
ATOM   1616  O  O     . ASN I  3 93  ? 67.617  81.003  120.119 1.00 17.42 ? 93   ASN A O     1 
ATOM   1617  C  CB    . ASN I  3 93  ? 68.308  81.936  117.222 1.00 22.05 ? 93   ASN A CB    1 
ATOM   1618  C  CG    . ASN I  3 93  ? 69.391  82.225  116.200 1.00 38.53 ? 93   ASN A CG    1 
ATOM   1619  O  OD1   . ASN I  3 93  ? 69.708  83.391  115.925 1.00 42.56 ? 93   ASN A OD1   1 
ATOM   1620  N  ND2   . ASN I  3 93  ? 69.972  81.170  115.637 1.00 44.44 ? 93   ASN A ND2   1 
ATOM   1621  N  N     . VAL I  3 94  ? 66.629  83.003  119.846 1.00 18.49 ? 94   VAL A N     1 
ATOM   1622  C  CA    . VAL I  3 94  ? 65.551  82.676  120.783 1.00 20.74 ? 94   VAL A CA    1 
ATOM   1623  C  C     . VAL I  3 94  ? 64.257  82.942  120.050 1.00 23.48 ? 94   VAL A C     1 
ATOM   1624  O  O     . VAL I  3 94  ? 64.079  84.022  119.487 1.00 24.13 ? 94   VAL A O     1 
ATOM   1625  C  CB    . VAL I  3 94  ? 65.584  83.584  122.032 1.00 20.68 ? 94   VAL A CB    1 
ATOM   1626  C  CG1   . VAL I  3 94  ? 64.431  83.199  122.992 1.00 21.78 ? 94   VAL A CG1   1 
ATOM   1627  C  CG2   . VAL I  3 94  ? 66.907  83.462  122.731 1.00 19.68 ? 94   VAL A CG2   1 
ATOM   1628  N  N     . LYS I  3 95  ? 63.348  81.983  120.022 1.00 22.44 ? 95   LYS A N     1 
ATOM   1629  C  CA    . LYS I  3 95  ? 62.109  82.255  119.332 1.00 25.99 ? 95   LYS A CA    1 
ATOM   1630  C  C     . LYS I  3 95  ? 60.888  81.495  119.781 1.00 26.50 ? 95   LYS A C     1 
ATOM   1631  O  O     . LYS I  3 95  ? 60.951  80.348  120.246 1.00 21.07 ? 95   LYS A O     1 
ATOM   1632  C  CB    . LYS I  3 95  ? 62.263  82.077  117.823 1.00 28.22 ? 95   LYS A CB    1 
ATOM   1633  C  CG    . LYS I  3 95  ? 62.292  80.638  117.364 1.00 28.78 ? 95   LYS A CG    1 
ATOM   1634  C  CD    . LYS I  3 95  ? 62.219  80.538  115.848 1.00 35.68 ? 95   LYS A CD    1 
ATOM   1635  C  CE    . LYS I  3 95  ? 62.213  79.087  115.407 1.00 37.29 ? 95   LYS A CE    1 
ATOM   1636  N  NZ    . LYS I  3 95  ? 62.301  78.928  113.923 1.00 40.11 ? 95   LYS A NZ    1 
ATOM   1637  N  N     . GLN I  3 96  ? 59.761  82.190  119.651 1.00 24.91 ? 96   GLN A N     1 
ATOM   1638  C  CA    . GLN I  3 96  ? 58.478  81.628  119.978 1.00 24.98 ? 96   GLN A CA    1 
ATOM   1639  C  C     . GLN I  3 96  ? 58.185  80.773  118.757 1.00 28.36 ? 96   GLN A C     1 
ATOM   1640  O  O     . GLN I  3 96  ? 58.242  81.252  117.613 1.00 30.97 ? 96   GLN A O     1 
ATOM   1641  C  CB    . GLN I  3 96  ? 57.462  82.755  120.159 1.00 24.85 ? 96   GLN A CB    1 
ATOM   1642  C  CG    . GLN I  3 96  ? 56.077  82.251  120.331 1.00 25.45 ? 96   GLN A CG    1 
ATOM   1643  C  CD    . GLN I  3 96  ? 55.065  83.356  120.513 1.00 22.13 ? 96   GLN A CD    1 
ATOM   1644  O  OE1   . GLN I  3 96  ? 55.295  84.512  120.139 1.00 23.19 ? 96   GLN A OE1   1 
ATOM   1645  N  NE2   . GLN I  3 96  ? 53.925  83.001  121.080 1.00 22.74 ? 96   GLN A NE2   1 
ATOM   1646  N  N     . VAL I  3 97  ? 57.900  79.500  118.978 1.00 27.80 ? 97   VAL A N     1 
ATOM   1647  C  CA    . VAL I  3 97  ? 57.680  78.606  117.859 1.00 33.51 ? 97   VAL A CA    1 
ATOM   1648  C  C     . VAL I  3 97  ? 56.345  78.698  117.136 1.00 40.40 ? 97   VAL A C     1 
ATOM   1649  O  O     . VAL I  3 97  ? 56.313  78.991  115.940 1.00 42.84 ? 97   VAL A O     1 
ATOM   1650  C  CB    . VAL I  3 97  ? 57.902  77.148  118.276 1.00 33.32 ? 97   VAL A CB    1 
ATOM   1651  C  CG1   . VAL I  3 97  ? 57.758  76.237  117.059 1.00 31.35 ? 97   VAL A CG1   1 
ATOM   1652  C  CG2   . VAL I  3 97  ? 59.289  76.996  118.885 1.00 32.63 ? 97   VAL A CG2   1 
ATOM   1653  N  N     . GLY I  3 98  ? 55.256  78.426  117.847 1.00 43.79 ? 98   GLY A N     1 
ATOM   1654  C  CA    . GLY I  3 98  ? 53.938  78.457  117.234 1.00 51.91 ? 98   GLY A CA    1 
ATOM   1655  C  C     . GLY I  3 98  ? 53.547  77.073  116.734 1.00 56.19 ? 98   GLY A C     1 
ATOM   1656  O  O     . GLY I  3 98  ? 54.222  76.520  115.866 1.00 58.17 ? 98   GLY A O     1 
ATOM   1657  N  N     . SER I  3 99  ? 52.463  76.516  117.280 1.00 59.39 ? 99   SER A N     1 
ATOM   1658  C  CA    . SER I  3 99  ? 51.976  75.179  116.905 1.00 60.04 ? 99   SER A CA    1 
ATOM   1659  C  C     . SER I  3 99  ? 51.974  74.924  115.396 1.00 60.04 ? 99   SER A C     1 
ATOM   1660  O  O     . SER I  3 99  ? 51.897  73.774  114.945 1.00 60.04 ? 99   SER A O     1 
ATOM   1661  C  CB    . SER I  3 99  ? 50.564  74.961  117.460 1.00 60.04 ? 99   SER A CB    1 
ATOM   1662  O  OG    . SER I  3 99  ? 49.661  75.943  116.974 1.00 60.04 ? 99   SER A OG    1 
ATOM   1663  N  N     . ARG I  3 100 ? 52.063  76.005  114.627 1.00 60.04 ? 100  ARG A N     1 
ATOM   1664  C  CA    . ARG I  3 100 ? 52.083  75.943  113.169 1.00 60.04 ? 100  ARG A CA    1 
ATOM   1665  C  C     . ARG I  3 100 ? 53.295  75.153  112.676 1.00 60.04 ? 100  ARG A C     1 
ATOM   1666  O  O     . ARG I  3 100 ? 53.284  74.606  111.569 1.00 60.04 ? 100  ARG A O     1 
ATOM   1667  C  CB    . ARG I  3 100 ? 52.138  77.368  112.612 1.00 59.84 ? 100  ARG A CB    1 
ATOM   1668  C  CG    . ARG I  3 100 ? 51.578  78.381  113.597 1.00 60.04 ? 100  ARG A CG    1 
ATOM   1669  C  CD    . ARG I  3 100 ? 51.348  79.767  113.015 1.00 59.76 ? 100  ARG A CD    1 
ATOM   1670  N  NE    . ARG I  3 100 ? 50.450  80.516  113.896 1.00 60.04 ? 100  ARG A NE    1 
ATOM   1671  C  CZ    . ARG I  3 100 ? 50.124  81.799  113.757 1.00 60.04 ? 100  ARG A CZ    1 
ATOM   1672  N  NH1   . ARG I  3 100 ? 50.618  82.524  112.760 1.00 60.04 ? 100  ARG A NH1   1 
ATOM   1673  N  NH2   . ARG I  3 100 ? 49.294  82.361  114.626 1.00 60.04 ? 100  ARG A NH2   1 
ATOM   1674  N  N     . ASN I  3 101 ? 54.332  75.094  113.513 1.00 60.04 ? 101  ASN A N     1 
ATOM   1675  C  CA    . ASN I  3 101 ? 55.582  74.409  113.178 1.00 60.04 ? 101  ASN A CA    1 
ATOM   1676  C  C     . ASN I  3 101 ? 55.697  72.921  113.513 1.00 60.04 ? 101  ASN A C     1 
ATOM   1677  O  O     . ASN I  3 101 ? 56.324  72.539  114.509 1.00 60.04 ? 101  ASN A O     1 
ATOM   1678  C  CB    . ASN I  3 101 ? 56.759  75.147  113.820 1.00 60.04 ? 101  ASN A CB    1 
ATOM   1679  C  CG    . ASN I  3 101 ? 57.419  76.127  112.873 1.00 60.04 ? 101  ASN A CG    1 
ATOM   1680  O  OD1   . ASN I  3 101 ? 57.797  75.764  111.755 1.00 60.04 ? 101  ASN A OD1   1 
ATOM   1681  N  ND2   . ASN I  3 101 ? 57.573  77.374  113.314 1.00 59.60 ? 101  ASN A ND2   1 
ATOM   1682  N  N     . ARG I  3 102 ? 55.107  72.078  112.677 1.00 58.55 ? 102  ARG A N     1 
ATOM   1683  C  CA    . ARG I  3 102 ? 55.201  70.643  112.893 1.00 58.19 ? 102  ARG A CA    1 
ATOM   1684  C  C     . ARG I  3 102 ? 56.599  70.257  112.402 1.00 56.02 ? 102  ARG A C     1 
ATOM   1685  O  O     . ARG I  3 102 ? 57.048  70.718  111.350 1.00 57.38 ? 102  ARG A O     1 
ATOM   1686  C  CB    . ARG I  3 102 ? 54.112  69.924  112.095 1.00 59.03 ? 102  ARG A CB    1 
ATOM   1687  C  CG    . ARG I  3 102 ? 52.712  70.428  112.438 1.00 60.04 ? 102  ARG A CG    1 
ATOM   1688  C  CD    . ARG I  3 102 ? 51.652  69.957  111.446 1.00 60.04 ? 102  ARG A CD    1 
ATOM   1689  N  NE    . ARG I  3 102 ? 50.408  70.724  111.582 1.00 60.04 ? 102  ARG A NE    1 
ATOM   1690  C  CZ    . ARG I  3 102 ? 49.353  70.596  110.781 1.00 60.04 ? 102  ARG A CZ    1 
ATOM   1691  N  NH1   . ARG I  3 102 ? 49.376  69.725  109.778 1.00 60.04 ? 102  ARG A NH1   1 
ATOM   1692  N  NH2   . ARG I  3 102 ? 48.278  71.352  110.973 1.00 60.04 ? 102  ARG A NH2   1 
ATOM   1693  N  N     . LEU I  3 103 ? 57.292  69.433  113.176 1.00 51.36 ? 103  LEU A N     1 
ATOM   1694  C  CA    . LEU I  3 103 ? 58.643  69.014  112.823 1.00 47.31 ? 103  LEU A CA    1 
ATOM   1695  C  C     . LEU I  3 103 ? 59.654  70.163  112.875 1.00 42.76 ? 103  LEU A C     1 
ATOM   1696  O  O     . LEU I  3 103 ? 60.735  70.066  112.296 1.00 39.32 ? 103  LEU A O     1 
ATOM   1697  C  CB    . LEU I  3 103 ? 58.678  68.359  111.434 1.00 47.80 ? 103  LEU A CB    1 
ATOM   1698  C  CG    . LEU I  3 103 ? 58.089  66.946  111.299 1.00 49.51 ? 103  LEU A CG    1 
ATOM   1699  C  CD1   . LEU I  3 103 ? 58.366  66.424  109.886 1.00 49.30 ? 103  LEU A CD1   1 
ATOM   1700  C  CD2   . LEU I  3 103 ? 58.700  66.006  112.342 1.00 46.37 ? 103  LEU A CD2   1 
ATOM   1701  N  N     . GLU I  3 104 ? 59.304  71.252  113.559 1.00 39.58 ? 104  GLU A N     1 
ATOM   1702  C  CA    . GLU I  3 104 ? 60.233  72.372  113.704 1.00 35.31 ? 104  GLU A CA    1 
ATOM   1703  C  C     . GLU I  3 104 ? 61.479  71.838  114.422 1.00 30.00 ? 104  GLU A C     1 
ATOM   1704  O  O     . GLU I  3 104 ? 62.600  72.201  114.063 1.00 26.29 ? 104  GLU A O     1 
ATOM   1705  C  CB    . GLU I  3 104 ? 59.603  73.499  114.536 1.00 37.76 ? 104  GLU A CB    1 
ATOM   1706  C  CG    . GLU I  3 104 ? 60.578  74.576  115.078 1.00 38.20 ? 104  GLU A CG    1 
ATOM   1707  C  CD    . GLU I  3 104 ? 61.187  75.461  113.999 1.00 43.47 ? 104  GLU A CD    1 
ATOM   1708  O  OE1   . GLU I  3 104 ? 60.607  75.553  112.891 1.00 45.11 ? 104  GLU A OE1   1 
ATOM   1709  O  OE2   . GLU I  3 104 ? 62.243  76.088  114.256 1.00 38.32 ? 104  GLU A OE2   1 
ATOM   1710  N  N     . ILE I  3 105 ? 61.290  70.971  115.419 1.00 30.37 ? 105  ILE A N     1 
ATOM   1711  C  CA    . ILE I  3 105 ? 62.455  70.444  116.132 1.00 30.36 ? 105  ILE A CA    1 
ATOM   1712  C  C     . ILE I  3 105 ? 63.366  69.602  115.256 1.00 25.97 ? 105  ILE A C     1 
ATOM   1713  O  O     . ILE I  3 105 ? 64.532  69.433  115.605 1.00 24.32 ? 105  ILE A O     1 
ATOM   1714  C  CB    . ILE I  3 105 ? 62.140  69.567  117.387 1.00 34.32 ? 105  ILE A CB    1 
ATOM   1715  C  CG1   . ILE I  3 105 ? 61.239  68.401  117.008 1.00 39.24 ? 105  ILE A CG1   1 
ATOM   1716  C  CG2   . ILE I  3 105 ? 61.592  70.419  118.515 1.00 40.13 ? 105  ILE A CG2   1 
ATOM   1717  C  CD1   . ILE I  3 105 ? 61.201  67.342  118.072 1.00 42.97 ? 105  ILE A CD1   1 
ATOM   1718  N  N     . ALA I  3 106 ? 62.851  69.075  114.140 1.00 27.02 ? 106  ALA A N     1 
ATOM   1719  C  CA    . ALA I  3 106 ? 63.706  68.273  113.256 1.00 24.30 ? 106  ALA A CA    1 
ATOM   1720  C  C     . ALA I  3 106 ? 64.665  69.151  112.464 1.00 24.10 ? 106  ALA A C     1 
ATOM   1721  O  O     . ALA I  3 106 ? 65.509  68.640  111.722 1.00 21.92 ? 106  ALA A O     1 
ATOM   1722  C  CB    . ALA I  3 106 ? 62.873  67.407  112.301 1.00 25.03 ? 106  ALA A CB    1 
ATOM   1723  N  N     . ARG I  3 107 ? 64.550  70.467  112.614 1.00 21.95 ? 107  ARG A N     1 
ATOM   1724  C  CA    . ARG I  3 107 ? 65.487  71.348  111.932 1.00 23.10 ? 107  ARG A CA    1 
ATOM   1725  C  C     . ARG I  3 107 ? 66.771  71.438  112.756 1.00 22.01 ? 107  ARG A C     1 
ATOM   1726  O  O     . ARG I  3 107 ? 67.750  72.041  112.317 1.00 25.40 ? 107  ARG A O     1 
ATOM   1727  C  CB    . ARG I  3 107 ? 64.897  72.753  111.765 1.00 27.69 ? 107  ARG A CB    1 
ATOM   1728  C  CG    . ARG I  3 107 ? 63.539  72.734  111.079 1.00 37.43 ? 107  ARG A CG    1 
ATOM   1729  C  CD    . ARG I  3 107 ? 63.198  74.049  110.397 1.00 45.61 ? 107  ARG A CD    1 
ATOM   1730  N  NE    . ARG I  3 107 ? 63.245  75.196  111.289 1.00 50.31 ? 107  ARG A NE    1 
ATOM   1731  C  CZ    . ARG I  3 107 ? 62.876  76.421  110.925 1.00 54.21 ? 107  ARG A CZ    1 
ATOM   1732  N  NH1   . ARG I  3 107 ? 62.439  76.637  109.693 1.00 55.91 ? 107  ARG A NH1   1 
ATOM   1733  N  NH2   . ARG I  3 107 ? 62.933  77.425  111.787 1.00 55.73 ? 107  ARG A NH2   1 
ATOM   1734  N  N     . TYR I  3 108 ? 66.772  70.813  113.937 1.00 19.28 ? 108  TYR A N     1 
ATOM   1735  C  CA    . TYR I  3 108 ? 67.933  70.862  114.821 1.00 19.40 ? 108  TYR A CA    1 
ATOM   1736  C  C     . TYR I  3 108 ? 68.611  69.516  114.925 1.00 20.14 ? 108  TYR A C     1 
ATOM   1737  O  O     . TYR I  3 108 ? 67.991  68.457  114.842 1.00 16.82 ? 108  TYR A O     1 
ATOM   1738  C  CB    . TYR I  3 108 ? 67.515  71.401  116.193 1.00 20.95 ? 108  TYR A CB    1 
ATOM   1739  C  CG    . TYR I  3 108 ? 66.829  72.722  115.986 1.00 21.82 ? 108  TYR A CG    1 
ATOM   1740  C  CD1   . TYR I  3 108 ? 65.450  72.819  116.042 1.00 22.78 ? 108  TYR A CD1   1 
ATOM   1741  C  CD2   . TYR I  3 108 ? 67.554  73.827  115.540 1.00 27.32 ? 108  TYR A CD2   1 
ATOM   1742  C  CE1   . TYR I  3 108 ? 64.787  74.000  115.633 1.00 25.90 ? 108  TYR A CE1   1 
ATOM   1743  C  CE2   . TYR I  3 108 ? 66.916  74.996  115.130 1.00 27.44 ? 108  TYR A CE2   1 
ATOM   1744  C  CZ    . TYR I  3 108 ? 65.531  75.072  115.174 1.00 25.87 ? 108  TYR A CZ    1 
ATOM   1745  O  OH    . TYR I  3 108 ? 64.893  76.205  114.712 1.00 31.27 ? 108  TYR A OH    1 
ATOM   1746  N  N     . GLN I  3 109 ? 69.911  69.586  115.095 1.00 20.59 ? 109  GLN A N     1 
ATOM   1747  C  CA    . GLN I  3 109 ? 70.738  68.413  115.088 1.00 20.89 ? 109  GLN A CA    1 
ATOM   1748  C  C     . GLN I  3 109 ? 70.315  67.191  115.879 1.00 16.47 ? 109  GLN A C     1 
ATOM   1749  O  O     . GLN I  3 109 ? 70.267  66.090  115.334 1.00 18.02 ? 109  GLN A O     1 
ATOM   1750  C  CB    . GLN I  3 109 ? 72.134  68.831  115.486 1.00 25.51 ? 109  GLN A CB    1 
ATOM   1751  C  CG    . GLN I  3 109 ? 73.174  67.992  114.867 1.00 31.30 ? 109  GLN A CG    1 
ATOM   1752  C  CD    . GLN I  3 109 ? 74.542  68.588  115.063 1.00 34.67 ? 109  GLN A CD    1 
ATOM   1753  O  OE1   . GLN I  3 109 ? 74.818  69.732  114.652 1.00 31.80 ? 109  GLN A OE1   1 
ATOM   1754  N  NE2   . GLN I  3 109 ? 75.412  67.828  115.702 1.00 36.63 ? 109  GLN A NE2   1 
ATOM   1755  N  N     . GLN I  3 110 ? 69.996  67.375  117.160 1.00 18.17 ? 110  GLN A N     1 
ATOM   1756  C  CA    . GLN I  3 110 ? 69.654  66.226  117.974 1.00 18.12 ? 110  GLN A CA    1 
ATOM   1757  C  C     . GLN I  3 110 ? 68.371  65.521  117.603 1.00 17.13 ? 110  GLN A C     1 
ATOM   1758  O  O     . GLN I  3 110 ? 68.144  64.408  118.058 1.00 15.94 ? 110  GLN A O     1 
ATOM   1759  C  CB    . GLN I  3 110 ? 69.578  66.606  119.461 1.00 17.39 ? 110  GLN A CB    1 
ATOM   1760  C  CG    . GLN I  3 110 ? 70.769  67.397  119.949 1.00 19.86 ? 110  GLN A CG    1 
ATOM   1761  C  CD    . GLN I  3 110 ? 70.445  68.861  120.051 1.00 21.84 ? 110  GLN A CD    1 
ATOM   1762  O  OE1   . GLN I  3 110 ? 70.156  69.526  119.043 1.00 18.49 ? 110  GLN A OE1   1 
ATOM   1763  N  NE2   . GLN I  3 110 ? 70.451  69.378  121.286 1.00 23.80 ? 110  GLN A NE2   1 
ATOM   1764  N  N     . TYR I  3 111 ? 67.529  66.148  116.776 1.00 15.93 ? 111  TYR A N     1 
ATOM   1765  C  CA    . TYR I  3 111 ? 66.251  65.538  116.398 1.00 15.53 ? 111  TYR A CA    1 
ATOM   1766  C  C     . TYR I  3 111 ? 65.995  65.501  114.884 1.00 14.37 ? 111  TYR A C     1 
ATOM   1767  O  O     . TYR I  3 111 ? 64.870  65.213  114.446 1.00 17.86 ? 111  TYR A O     1 
ATOM   1768  C  CB    . TYR I  3 111 ? 65.106  66.303  117.076 1.00 14.91 ? 111  TYR A CB    1 
ATOM   1769  C  CG    . TYR I  3 111 ? 65.236  66.331  118.598 1.00 14.73 ? 111  TYR A CG    1 
ATOM   1770  C  CD1   . TYR I  3 111 ? 65.835  67.410  119.245 1.00 14.53 ? 111  TYR A CD1   1 
ATOM   1771  C  CD2   . TYR I  3 111 ? 64.873  65.220  119.360 1.00 15.21 ? 111  TYR A CD2   1 
ATOM   1772  C  CE1   . TYR I  3 111 ? 66.077  67.384  120.634 1.00 15.63 ? 111  TYR A CE1   1 
ATOM   1773  C  CE2   . TYR I  3 111 ? 65.122  65.175  120.756 1.00 15.13 ? 111  TYR A CE2   1 
ATOM   1774  C  CZ    . TYR I  3 111 ? 65.718  66.254  121.366 1.00 15.66 ? 111  TYR A CZ    1 
ATOM   1775  O  OH    . TYR I  3 111 ? 66.012  66.207  122.705 1.00 14.92 ? 111  TYR A OH    1 
ATOM   1776  N  N     . ALA I  3 112 ? 67.037  65.743  114.103 1.00 18.06 ? 112  ALA A N     1 
ATOM   1777  C  CA    . ALA I  3 112 ? 66.881  65.775  112.636 1.00 18.65 ? 112  ALA A CA    1 
ATOM   1778  C  C     . ALA I  3 112 ? 66.364  64.465  112.054 1.00 18.83 ? 112  ALA A C     1 
ATOM   1779  O  O     . ALA I  3 112 ? 65.711  64.470  111.010 1.00 22.95 ? 112  ALA A O     1 
ATOM   1780  C  CB    . ALA I  3 112 ? 68.207  66.148  111.993 1.00 22.84 ? 112  ALA A CB    1 
ATOM   1781  N  N     . HIS I  3 113 ? 66.644  63.339  112.708 1.00 18.62 ? 113  HIS A N     1 
ATOM   1782  C  CA    . HIS I  3 113 ? 66.168  62.056  112.208 1.00 18.32 ? 113  HIS A CA    1 
ATOM   1783  C  C     . HIS I  3 113 ? 64.657  61.870  112.261 1.00 20.14 ? 113  HIS A C     1 
ATOM   1784  O  O     . HIS I  3 113 ? 64.141  60.934  111.669 1.00 23.04 ? 113  HIS A O     1 
ATOM   1785  C  CB    . HIS I  3 113 ? 66.810  60.895  112.986 1.00 18.89 ? 113  HIS A CB    1 
ATOM   1786  C  CG    . HIS I  3 113 ? 66.602  60.983  114.467 1.00 17.42 ? 113  HIS A CG    1 
ATOM   1787  N  ND1   . HIS I  3 113 ? 67.179  61.977  115.224 1.00 19.63 ? 113  HIS A ND1   1 
ATOM   1788  C  CD2   . HIS I  3 113 ? 65.900  60.207  115.331 1.00 18.95 ? 113  HIS A CD2   1 
ATOM   1789  C  CE1   . HIS I  3 113 ? 66.849  61.813  116.493 1.00 16.12 ? 113  HIS A CE1   1 
ATOM   1790  N  NE2   . HIS I  3 113 ? 66.076  60.749  116.587 1.00 17.85 ? 113  HIS A NE2   1 
ATOM   1791  N  N     . LEU I  3 114 ? 63.942  62.733  112.980 1.00 19.76 ? 114  LEU A N     1 
ATOM   1792  C  CA    . LEU I  3 114 ? 62.501  62.593  113.040 1.00 22.01 ? 114  LEU A CA    1 
ATOM   1793  C  C     . LEU I  3 114 ? 61.885  62.852  111.658 1.00 21.90 ? 114  LEU A C     1 
ATOM   1794  O  O     . LEU I  3 114 ? 60.817  62.324  111.341 1.00 23.02 ? 114  LEU A O     1 
ATOM   1795  C  CB    . LEU I  3 114 ? 61.917  63.533  114.096 1.00 23.49 ? 114  LEU A CB    1 
ATOM   1796  C  CG    . LEU I  3 114 ? 62.325  63.176  115.538 1.00 27.04 ? 114  LEU A CG    1 
ATOM   1797  C  CD1   . LEU I  3 114 ? 61.566  64.096  116.472 1.00 28.86 ? 114  LEU A CD1   1 
ATOM   1798  C  CD2   . LEU I  3 114 ? 62.030  61.719  115.864 1.00 27.56 ? 114  LEU A CD2   1 
ATOM   1799  N  N     . THR I  3 115 ? 62.570  63.632  110.828 1.00 23.99 ? 115  THR A N     1 
ATOM   1800  C  CA    . THR I  3 115 ? 62.068  63.884  109.462 1.00 24.70 ? 115  THR A CA    1 
ATOM   1801  C  C     . THR I  3 115 ? 62.059  62.565  108.687 1.00 25.43 ? 115  THR A C     1 
ATOM   1802  O  O     . THR I  3 115 ? 61.096  62.248  107.978 1.00 25.51 ? 115  THR A O     1 
ATOM   1803  C  CB    . THR I  3 115 ? 62.955  64.888  108.674 1.00 27.40 ? 115  THR A CB    1 
ATOM   1804  O  OG1   . THR I  3 115 ? 62.860  66.192  109.264 1.00 26.30 ? 115  THR A OG1   1 
ATOM   1805  C  CG2   . THR I  3 115 ? 62.482  64.991  107.214 1.00 26.70 ? 115  THR A CG2   1 
ATOM   1806  N  N     . ALA I  3 116 ? 63.135  61.794  108.807 1.00 23.36 ? 116  ALA A N     1 
ATOM   1807  C  CA    . ALA I  3 116 ? 63.212  60.520  108.097 1.00 26.21 ? 116  ALA A CA    1 
ATOM   1808  C  C     . ALA I  3 116 ? 62.153  59.543  108.610 1.00 28.35 ? 116  ALA A C     1 
ATOM   1809  O  O     . ALA I  3 116 ? 61.512  58.824  107.821 1.00 28.52 ? 116  ALA A O     1 
ATOM   1810  C  CB    . ALA I  3 116 ? 64.607  59.925  108.241 1.00 25.37 ? 116  ALA A CB    1 
ATOM   1811  N  N     . LEU I  3 117 ? 61.945  59.533  109.923 1.00 26.89 ? 117  LEU A N     1 
ATOM   1812  C  CA    . LEU I  3 117 ? 60.948  58.652  110.532 1.00 29.12 ? 117  LEU A CA    1 
ATOM   1813  C  C     . LEU I  3 117 ? 59.564  59.000  109.994 1.00 29.19 ? 117  LEU A C     1 
ATOM   1814  O  O     . LEU I  3 117 ? 58.809  58.124  109.569 1.00 29.78 ? 117  LEU A O     1 
ATOM   1815  C  CB    . LEU I  3 117 ? 60.937  58.812  112.051 1.00 28.62 ? 117  LEU A CB    1 
ATOM   1816  C  CG    . LEU I  3 117 ? 62.147  58.297  112.826 1.00 36.27 ? 117  LEU A CG    1 
ATOM   1817  C  CD1   . LEU I  3 117 ? 61.906  58.469  114.315 1.00 36.37 ? 117  LEU A CD1   1 
ATOM   1818  C  CD2   . LEU I  3 117 ? 62.361  56.842  112.502 1.00 40.63 ? 117  LEU A CD2   1 
ATOM   1819  N  N     . ALA I  3 118 ? 59.248  60.288  110.029 1.00 26.84 ? 118  ALA A N     1 
ATOM   1820  C  CA    . ALA I  3 118 ? 57.970  60.786  109.552 1.00 30.01 ? 118  ALA A CA    1 
ATOM   1821  C  C     . ALA I  3 118 ? 57.778  60.429  108.077 1.00 31.74 ? 118  ALA A C     1 
ATOM   1822  O  O     . ALA I  3 118 ? 56.703  59.969  107.688 1.00 34.28 ? 118  ALA A O     1 
ATOM   1823  C  CB    . ALA I  3 118 ? 57.904  62.296  109.749 1.00 28.34 ? 118  ALA A CB    1 
ATOM   1824  N  N     . LYS I  3 119 ? 58.811  60.636  107.264 1.00 33.60 ? 119  LYS A N     1 
ATOM   1825  C  CA    . LYS I  3 119 ? 58.732  60.328  105.833 1.00 37.68 ? 119  LYS A CA    1 
ATOM   1826  C  C     . LYS I  3 119 ? 58.536  58.842  105.582 1.00 39.56 ? 119  LYS A C     1 
ATOM   1827  O  O     . LYS I  3 119 ? 57.828  58.451  104.648 1.00 40.18 ? 119  LYS A O     1 
ATOM   1828  C  CB    . LYS I  3 119 ? 59.992  60.792  105.091 1.00 40.63 ? 119  LYS A CB    1 
ATOM   1829  C  CG    . LYS I  3 119 ? 60.063  62.296  104.831 1.00 46.03 ? 119  LYS A CG    1 
ATOM   1830  C  CD    . LYS I  3 119 ? 61.412  62.698  104.226 1.00 49.03 ? 119  LYS A CD    1 
ATOM   1831  C  CE    . LYS I  3 119 ? 61.453  64.191  103.889 1.00 50.89 ? 119  LYS A CE    1 
ATOM   1832  N  NZ    . LYS I  3 119 ? 62.781  64.632  103.359 1.00 51.70 ? 119  LYS A NZ    1 
ATOM   1833  N  N     . ALA I  3 120 ? 59.157  58.010  106.409 1.00 38.60 ? 120  ALA A N     1 
ATOM   1834  C  CA    . ALA I  3 120 ? 59.020  56.569  106.237 1.00 40.83 ? 120  ALA A CA    1 
ATOM   1835  C  C     . ALA I  3 120 ? 57.630  56.094  106.671 1.00 41.71 ? 120  ALA A C     1 
ATOM   1836  O  O     . ALA I  3 120 ? 57.044  55.211  106.043 1.00 42.56 ? 120  ALA A O     1 
ATOM   1837  C  CB    . ALA I  3 120 ? 60.103  55.839  107.025 1.00 40.57 ? 120  ALA A CB    1 
ATOM   1838  N  N     . ALA I  3 121 ? 57.107  56.684  107.741 1.00 40.37 ? 121  ALA A N     1 
ATOM   1839  C  CA    . ALA I  3 121 ? 55.784  56.326  108.245 1.00 43.27 ? 121  ALA A CA    1 
ATOM   1840  C  C     . ALA I  3 121 ? 54.684  56.706  107.251 1.00 47.56 ? 121  ALA A C     1 
ATOM   1841  O  O     . ALA I  3 121 ? 53.691  55.991  107.113 1.00 48.41 ? 121  ALA A O     1 
ATOM   1842  C  CB    . ALA I  3 121 ? 55.527  57.008  109.591 1.00 38.73 ? 121  ALA A CB    1 
ATOM   1843  N  N     . GLU I  3 122 ? 54.856  57.825  106.555 1.00 49.24 ? 122  GLU A N     1 
ATOM   1844  C  CA    . GLU I  3 122 ? 53.847  58.258  105.596 1.00 54.11 ? 122  GLU A CA    1 
ATOM   1845  C  C     . GLU I  3 122 ? 53.735  57.248  104.460 1.00 54.66 ? 122  GLU A C     1 
ATOM   1846  O  O     . GLU I  3 122 ? 53.182  57.540  103.397 1.00 56.73 ? 122  GLU A O     1 
ATOM   1847  C  CB    . GLU I  3 122 ? 54.196  59.634  105.028 1.00 55.09 ? 122  GLU A CB    1 
ATOM   1848  C  CG    . GLU I  3 122 ? 55.403  59.625  104.122 1.00 59.54 ? 122  GLU A CG    1 
ATOM   1849  C  CD    . GLU I  3 122 ? 55.723  60.996  103.567 1.00 60.04 ? 122  GLU A CD    1 
ATOM   1850  O  OE1   . GLU I  3 122 ? 55.893  61.937  104.375 1.00 60.04 ? 122  GLU A OE1   1 
ATOM   1851  O  OE2   . GLU I  3 122 ? 55.807  61.133  102.325 1.00 60.04 ? 122  GLU A OE2   1 
ATOM   1852  N  N     . GLU I  3 123 ? 54.273  56.058  104.687 1.00 54.10 ? 123  GLU A N     1 
ATOM   1853  C  CA    . GLU I  3 123 ? 54.220  55.000  103.690 1.00 53.73 ? 123  GLU A CA    1 
ATOM   1854  C  C     . GLU I  3 123 ? 54.154  53.648  104.386 1.00 51.66 ? 123  GLU A C     1 
ATOM   1855  O  O     . GLU I  3 123 ? 54.103  52.612  103.732 1.00 51.94 ? 123  GLU A O     1 
ATOM   1856  C  CB    . GLU I  3 123 ? 55.459  55.064  102.792 1.00 54.72 ? 123  GLU A CB    1 
ATOM   1857  C  CG    . GLU I  3 123 ? 55.737  56.454  102.228 1.00 56.89 ? 123  GLU A CG    1 
ATOM   1858  C  CD    . GLU I  3 123 ? 57.061  56.531  101.485 1.00 60.04 ? 123  GLU A CD    1 
ATOM   1859  O  OE1   . GLU I  3 123 ? 58.099  56.146  102.068 1.00 59.36 ? 123  GLU A OE1   1 
ATOM   1860  O  OE2   . GLU I  3 123 ? 57.070  56.982  100.317 1.00 60.04 ? 123  GLU A OE2   1 
ATOM   1861  N  N     . ASN I  3 124 ? 54.139  53.664  105.719 1.00 50.05 ? 124  ASN A N     1 
ATOM   1862  C  CA    . ASN I  3 124 ? 54.103  52.426  106.474 1.00 48.89 ? 124  ASN A CA    1 
ATOM   1863  C  C     . ASN I  3 124 ? 53.298  52.413  107.779 1.00 49.44 ? 124  ASN A C     1 
ATOM   1864  O  O     . ASN I  3 124 ? 53.718  52.968  108.796 1.00 43.48 ? 124  ASN A O     1 
ATOM   1865  C  CB    . ASN I  3 124 ? 55.531  51.964  106.778 1.00 52.29 ? 124  ASN A CB    1 
ATOM   1866  C  CG    . ASN I  3 124 ? 55.559  50.717  107.628 1.00 54.58 ? 124  ASN A CG    1 
ATOM   1867  O  OD1   . ASN I  3 124 ? 54.516  50.166  107.966 1.00 54.31 ? 124  ASN A OD1   1 
ATOM   1868  N  ND2   . ASN I  3 124 ? 56.759  50.258  107.976 1.00 58.29 ? 124  ASN A ND2   1 
ATOM   1869  N  N     . PRO I  3 125 ? 52.141  51.725  107.754 1.00 50.64 ? 125  PRO A N     1 
ATOM   1870  C  CA    . PRO I  3 125 ? 51.143  51.500  108.811 1.00 50.38 ? 125  PRO A CA    1 
ATOM   1871  C  C     . PRO I  3 125 ? 51.625  51.301  110.271 1.00 50.43 ? 125  PRO A C     1 
ATOM   1872  O  O     . PRO I  3 125 ? 51.722  52.269  111.014 1.00 46.41 ? 125  PRO A O     1 
ATOM   1873  C  CB    . PRO I  3 125 ? 50.361  50.290  108.272 1.00 53.30 ? 125  PRO A CB    1 
ATOM   1874  C  CG    . PRO I  3 125 ? 51.265  49.734  107.119 1.00 53.64 ? 125  PRO A CG    1 
ATOM   1875  C  CD    . PRO I  3 125 ? 51.751  51.008  106.539 1.00 48.66 ? 125  PRO A CD    1 
ATOM   1876  N  N     . GLU I  3 126 ? 51.918  50.068  110.693 1.00 55.02 ? 126  GLU A N     1 
ATOM   1877  C  CA    . GLU I  3 126 ? 52.349  49.838  112.085 1.00 54.75 ? 126  GLU A CA    1 
ATOM   1878  C  C     . GLU I  3 126 ? 53.663  50.515  112.422 1.00 54.65 ? 126  GLU A C     1 
ATOM   1879  O  O     . GLU I  3 126 ? 54.189  50.379  113.538 1.00 55.10 ? 126  GLU A O     1 
ATOM   1880  C  CB    . GLU I  3 126 ? 52.420  48.342  112.421 1.00 58.70 ? 126  GLU A CB    1 
ATOM   1881  C  CG    . GLU I  3 126 ? 52.470  48.058  113.939 1.00 58.50 ? 126  GLU A CG    1 
ATOM   1882  C  CD    . GLU I  3 126 ? 51.722  46.782  114.319 1.00 60.04 ? 126  GLU A CD    1 
ATOM   1883  O  OE1   . GLU I  3 126 ? 51.636  45.881  113.451 1.00 60.04 ? 126  GLU A OE1   1 
ATOM   1884  O  OE2   . GLU I  3 126 ? 51.231  46.669  115.475 1.00 53.98 ? 126  GLU A OE2   1 
ATOM   1885  N  N     . LEU I  3 127 ? 54.200  51.232  111.438 1.00 53.30 ? 127  LEU A N     1 
ATOM   1886  C  CA    . LEU I  3 127 ? 55.411  51.997  111.650 1.00 51.86 ? 127  LEU A CA    1 
ATOM   1887  C  C     . LEU I  3 127 ? 54.814  53.213  112.350 1.00 51.69 ? 127  LEU A C     1 
ATOM   1888  O  O     . LEU I  3 127 ? 55.320  53.684  113.367 1.00 51.32 ? 127  LEU A O     1 
ATOM   1889  C  CB    . LEU I  3 127 ? 56.028  52.421  110.313 1.00 52.83 ? 127  LEU A CB    1 
ATOM   1890  C  CG    . LEU I  3 127 ? 57.506  52.107  110.034 1.00 55.59 ? 127  LEU A CG    1 
ATOM   1891  C  CD1   . LEU I  3 127 ? 57.971  52.936  108.833 1.00 53.22 ? 127  LEU A CD1   1 
ATOM   1892  C  CD2   . LEU I  3 127 ? 58.366  52.427  111.257 1.00 55.31 ? 127  LEU A CD2   1 
ATOM   1893  N  N     . ALA I  3 128 ? 53.690  53.676  111.799 1.00 49.35 ? 128  ALA A N     1 
ATOM   1894  C  CA    . ALA I  3 128 ? 52.980  54.830  112.324 1.00 47.74 ? 128  ALA A CA    1 
ATOM   1895  C  C     . ALA I  3 128 ? 52.355  54.549  113.689 1.00 46.60 ? 128  ALA A C     1 
ATOM   1896  O  O     . ALA I  3 128 ? 52.435  55.376  114.599 1.00 44.03 ? 128  ALA A O     1 
ATOM   1897  C  CB    . ALA I  3 128 ? 51.900  55.273  111.327 1.00 48.79 ? 128  ALA A CB    1 
ATOM   1898  N  N     . ALA I  3 129 ? 51.731  53.387  113.838 1.00 44.66 ? 129  ALA A N     1 
ATOM   1899  C  CA    . ALA I  3 129 ? 51.095  53.046  115.110 1.00 45.09 ? 129  ALA A CA    1 
ATOM   1900  C  C     . ALA I  3 129 ? 52.109  52.935  116.249 1.00 46.05 ? 129  ALA A C     1 
ATOM   1901  O  O     . ALA I  3 129 ? 51.857  53.398  117.370 1.00 46.02 ? 129  ALA A O     1 
ATOM   1902  C  CB    . ALA I  3 129 ? 50.319  51.736  114.974 1.00 45.96 ? 129  ALA A CB    1 
ATOM   1903  N  N     . ALA I  3 130 ? 53.258  52.338  115.942 1.00 46.84 ? 130  ALA A N     1 
ATOM   1904  C  CA    . ALA I  3 130 ? 54.324  52.125  116.920 1.00 48.44 ? 130  ALA A CA    1 
ATOM   1905  C  C     . ALA I  3 130 ? 55.138  53.372  117.254 1.00 49.19 ? 130  ALA A C     1 
ATOM   1906  O  O     . ALA I  3 130 ? 55.444  53.637  118.421 1.00 48.35 ? 130  ALA A O     1 
ATOM   1907  C  CB    . ALA I  3 130 ? 55.253  51.017  116.423 1.00 49.61 ? 130  ALA A CB    1 
ATOM   1908  N  N     . LEU I  3 131 ? 55.496  54.134  116.227 1.00 50.91 ? 131  LEU A N     1 
ATOM   1909  C  CA    . LEU I  3 131 ? 56.286  55.352  116.413 1.00 52.28 ? 131  LEU A CA    1 
ATOM   1910  C  C     . LEU I  3 131 ? 55.438  56.480  116.996 1.00 53.60 ? 131  LEU A C     1 
ATOM   1911  O  O     . LEU I  3 131 ? 55.911  57.278  117.808 1.00 54.89 ? 131  LEU A O     1 
ATOM   1912  C  CB    . LEU I  3 131 ? 56.882  55.790  115.067 1.00 53.56 ? 131  LEU A CB    1 
ATOM   1913  C  CG    . LEU I  3 131 ? 57.708  54.738  114.308 1.00 54.18 ? 131  LEU A CG    1 
ATOM   1914  C  CD1   . LEU I  3 131 ? 57.974  55.209  112.880 1.00 54.98 ? 131  LEU A CD1   1 
ATOM   1915  C  CD2   . LEU I  3 131 ? 59.016  54.475  115.049 1.00 55.32 ? 131  LEU A CD2   1 
ATOM   1916  N  N     . GLY I  3 132 ? 54.178  56.539  116.582 1.00 53.66 ? 132  GLY A N     1 
ATOM   1917  C  CA    . GLY I  3 132 ? 53.306  57.584  117.072 1.00 55.87 ? 132  GLY A CA    1 
ATOM   1918  C  C     . GLY I  3 132 ? 53.483  58.842  116.250 1.00 57.66 ? 132  GLY A C     1 
ATOM   1919  O  O     . GLY I  3 132 ? 53.999  58.786  115.132 1.00 58.86 ? 132  GLY A O     1 
ATOM   1920  N  N     . SER I  3 133 ? 53.046  59.972  116.796 1.00 58.81 ? 133  SER A N     1 
ATOM   1921  C  CA    . SER I  3 133 ? 53.157  61.260  116.115 1.00 59.65 ? 133  SER A CA    1 
ATOM   1922  C  C     . SER I  3 133 ? 53.487  62.338  117.137 1.00 59.94 ? 133  SER A C     1 
ATOM   1923  O  O     . SER I  3 133 ? 53.706  63.494  116.781 1.00 58.57 ? 133  SER A O     1 
ATOM   1924  C  CB    . SER I  3 133 ? 51.845  61.623  115.395 1.00 60.04 ? 133  SER A CB    1 
ATOM   1925  O  OG    . SER I  3 133 ? 50.827  62.016  116.310 1.00 60.04 ? 133  SER A OG    1 
ATOM   1926  N  N     . ASP I  3 134 ? 53.497  61.957  118.413 1.00 60.04 ? 134  ASP A N     1 
ATOM   1927  C  CA    . ASP I  3 134 ? 53.823  62.903  119.473 1.00 60.04 ? 134  ASP A CA    1 
ATOM   1928  C  C     . ASP I  3 134 ? 55.290  63.278  119.326 1.00 60.04 ? 134  ASP A C     1 
ATOM   1929  O  O     . ASP I  3 134 ? 55.686  64.386  119.705 1.00 60.04 ? 134  ASP A O     1 
ATOM   1930  C  CB    . ASP I  3 134 ? 53.560  62.290  120.857 1.00 60.04 ? 134  ASP A CB    1 
ATOM   1931  C  CG    . ASP I  3 134 ? 52.260  62.793  121.486 1.00 60.04 ? 134  ASP A CG    1 
ATOM   1932  O  OD1   . ASP I  3 134 ? 51.251  62.913  120.752 1.00 57.36 ? 134  ASP A OD1   1 
ATOM   1933  O  OD2   . ASP I  3 134 ? 52.246  63.057  122.716 1.00 58.26 ? 134  ASP A OD2   1 
ATOM   1934  N  N     . TYR I  3 135 ? 56.090  62.366  118.757 1.00 60.04 ? 135  TYR A N     1 
ATOM   1935  C  CA    . TYR I  3 135 ? 57.506  62.647  118.558 1.00 60.01 ? 135  TYR A CA    1 
ATOM   1936  C  C     . TYR I  3 135 ? 57.551  63.950  117.784 1.00 60.04 ? 135  TYR A C     1 
ATOM   1937  O  O     . TYR I  3 135 ? 58.607  64.555  117.597 1.00 60.04 ? 135  TYR A O     1 
ATOM   1938  C  CB    . TYR I  3 135 ? 58.238  61.508  117.821 1.00 59.39 ? 135  TYR A CB    1 
ATOM   1939  C  CG    . TYR I  3 135 ? 57.784  61.167  116.416 1.00 60.04 ? 135  TYR A CG    1 
ATOM   1940  C  CD1   . TYR I  3 135 ? 57.785  62.121  115.394 1.00 60.04 ? 135  TYR A CD1   1 
ATOM   1941  C  CD2   . TYR I  3 135 ? 57.430  59.857  116.089 1.00 60.04 ? 135  TYR A CD2   1 
ATOM   1942  C  CE1   . TYR I  3 135 ? 57.448  61.774  114.080 1.00 60.04 ? 135  TYR A CE1   1 
ATOM   1943  C  CE2   . TYR I  3 135 ? 57.093  59.501  114.784 1.00 60.04 ? 135  TYR A CE2   1 
ATOM   1944  C  CZ    . TYR I  3 135 ? 57.104  60.460  113.786 1.00 60.04 ? 135  TYR A CZ    1 
ATOM   1945  O  OH    . TYR I  3 135 ? 56.760  60.095  112.506 1.00 60.04 ? 135  TYR A OH    1 
ATOM   1946  N  N     . THR I  3 136 ? 56.368  64.359  117.335 1.00 59.85 ? 136  THR A N     1 
ATOM   1947  C  CA    . THR I  3 136 ? 56.179  65.625  116.663 1.00 58.55 ? 136  THR A CA    1 
ATOM   1948  C  C     . THR I  3 136 ? 56.086  66.563  117.871 1.00 56.10 ? 136  THR A C     1 
ATOM   1949  O  O     . THR I  3 136 ? 54.999  66.959  118.308 1.00 57.49 ? 136  THR A O     1 
ATOM   1950  C  CB    . THR I  3 136 ? 54.854  65.640  115.855 1.00 59.95 ? 136  THR A CB    1 
ATOM   1951  O  OG1   . THR I  3 136 ? 54.993  64.799  114.701 1.00 60.02 ? 136  THR A OG1   1 
ATOM   1952  C  CG2   . THR I  3 136 ? 54.493  67.051  115.413 1.00 60.03 ? 136  THR A CG2   1 
ATOM   1953  N  N     . ILE I  3 137 ? 57.252  66.858  118.432 1.00 50.43 ? 137  ILE A N     1 
ATOM   1954  C  CA    . ILE I  3 137 ? 57.385  67.725  119.597 1.00 46.29 ? 137  ILE A CA    1 
ATOM   1955  C  C     . ILE I  3 137 ? 57.415  69.166  119.100 1.00 43.01 ? 137  ILE A C     1 
ATOM   1956  O  O     . ILE I  3 137 ? 58.087  69.476  118.112 1.00 43.15 ? 137  ILE A O     1 
ATOM   1957  C  CB    . ILE I  3 137 ? 58.700  67.406  120.343 1.00 46.89 ? 137  ILE A CB    1 
ATOM   1958  C  CG1   . ILE I  3 137 ? 59.088  65.944  120.074 1.00 43.55 ? 137  ILE A CG1   1 
ATOM   1959  C  CG2   . ILE I  3 137 ? 58.521  67.623  121.857 1.00 45.89 ? 137  ILE A CG2   1 
ATOM   1960  C  CD1   . ILE I  3 137 ? 60.406  65.522  120.672 1.00 48.13 ? 137  ILE A CD1   1 
ATOM   1961  N  N     . THR I  3 138 ? 56.680  70.042  119.770 1.00 39.44 ? 138  THR A N     1 
ATOM   1962  C  CA    . THR I  3 138 ? 56.625  71.447  119.369 1.00 37.60 ? 138  THR A CA    1 
ATOM   1963  C  C     . THR I  3 138 ? 56.713  72.334  120.608 1.00 30.00 ? 138  THR A C     1 
ATOM   1964  O  O     . THR I  3 138 ? 55.682  72.735  121.157 1.00 32.02 ? 138  THR A O     1 
ATOM   1965  C  CB    . THR I  3 138 ? 55.295  71.760  118.637 1.00 41.03 ? 138  THR A CB    1 
ATOM   1966  O  OG1   . THR I  3 138 ? 55.119  70.843  117.545 1.00 44.22 ? 138  THR A OG1   1 
ATOM   1967  C  CG2   . THR I  3 138 ? 55.306  73.191  118.101 1.00 43.81 ? 138  THR A CG2   1 
ATOM   1968  N  N     . PRO I  3 139 ? 57.937  72.645  121.070 1.00 25.42 ? 139  PRO A N     1 
ATOM   1969  C  CA    . PRO I  3 139 ? 58.072  73.494  122.260 1.00 22.21 ? 139  PRO A CA    1 
ATOM   1970  C  C     . PRO I  3 139 ? 57.451  74.860  122.037 1.00 22.14 ? 139  PRO A C     1 
ATOM   1971  O  O     . PRO I  3 139 ? 57.277  75.285  120.902 1.00 23.31 ? 139  PRO A O     1 
ATOM   1972  C  CB    . PRO I  3 139 ? 59.585  73.579  122.475 1.00 23.22 ? 139  PRO A CB    1 
ATOM   1973  C  CG    . PRO I  3 139 ? 60.115  72.296  121.794 1.00 23.62 ? 139  PRO A CG    1 
ATOM   1974  C  CD    . PRO I  3 139 ? 59.255  72.254  120.553 1.00 24.29 ? 139  PRO A CD    1 
ATOM   1975  N  N     . ASP I  3 140 ? 57.100  75.551  123.114 1.00 19.42 ? 140  ASP A N     1 
ATOM   1976  C  CA    . ASP I  3 140 ? 56.506  76.884  122.984 1.00 16.09 ? 140  ASP A CA    1 
ATOM   1977  C  C     . ASP I  3 140 ? 57.564  77.884  122.517 1.00 16.07 ? 140  ASP A C     1 
ATOM   1978  O  O     . ASP I  3 140 ? 57.312  78.705  121.629 1.00 17.90 ? 140  ASP A O     1 
ATOM   1979  C  CB    . ASP I  3 140 ? 55.949  77.350  124.339 1.00 17.20 ? 140  ASP A CB    1 
ATOM   1980  C  CG    . ASP I  3 140 ? 54.786  76.523  124.795 1.00 20.15 ? 140  ASP A CG    1 
ATOM   1981  O  OD1   . ASP I  3 140 ? 54.220  75.808  123.943 1.00 17.66 ? 140  ASP A OD1   1 
ATOM   1982  O  OD2   . ASP I  3 140 ? 54.422  76.605  125.999 1.00 18.09 ? 140  ASP A OD2   1 
ATOM   1983  N  N     . ILE I  3 141 ? 58.733  77.811  123.146 1.00 15.37 ? 141  ILE A N     1 
ATOM   1984  C  CA    . ILE I  3 141 ? 59.870  78.684  122.855 1.00 14.91 ? 141  ILE A CA    1 
ATOM   1985  C  C     . ILE I  3 141 ? 61.115  77.823  122.764 1.00 16.24 ? 141  ILE A C     1 
ATOM   1986  O  O     . ILE I  3 141 ? 61.293  76.902  123.539 1.00 16.86 ? 141  ILE A O     1 
ATOM   1987  C  CB    . ILE I  3 141 ? 60.133  79.698  124.013 1.00 15.25 ? 141  ILE A CB    1 
ATOM   1988  C  CG1   . ILE I  3 141 ? 58.945  80.656  124.159 1.00 17.15 ? 141  ILE A CG1   1 
ATOM   1989  C  CG2   . ILE I  3 141 ? 61.420  80.508  123.758 1.00 16.36 ? 141  ILE A CG2   1 
ATOM   1990  C  CD1   . ILE I  3 141 ? 59.011  81.477  125.440 1.00 15.71 ? 141  ILE A CD1   1 
ATOM   1991  N  N     . ILE I  3 142 ? 61.986  78.130  121.814 1.00 15.36 ? 142  ILE A N     1 
ATOM   1992  C  CA    . ILE I  3 142 ? 63.222  77.381  121.736 1.00 14.86 ? 142  ILE A CA    1 
ATOM   1993  C  C     . ILE I  3 142 ? 64.394  78.341  121.685 1.00 17.55 ? 142  ILE A C     1 
ATOM   1994  O  O     . ILE I  3 142 ? 64.255  79.496  121.242 1.00 17.44 ? 142  ILE A O     1 
ATOM   1995  C  CB    . ILE I  3 142 ? 63.321  76.442  120.477 1.00 14.49 ? 142  ILE A CB    1 
ATOM   1996  C  CG1   . ILE I  3 142 ? 63.197  77.255  119.182 1.00 15.97 ? 142  ILE A CG1   1 
ATOM   1997  C  CG2   . ILE I  3 142 ? 62.312  75.316  120.580 1.00 15.37 ? 142  ILE A CG2   1 
ATOM   1998  C  CD1   . ILE I  3 142 ? 63.323  76.403  117.894 1.00 18.64 ? 142  ILE A CD1   1 
ATOM   1999  N  N     . VAL I  3 143 ? 65.528  77.882  122.214 1.00 16.93 ? 143  VAL A N     1 
ATOM   2000  C  CA    . VAL I  3 143 ? 66.788  78.620  122.117 1.00 14.08 ? 143  VAL A CA    1 
ATOM   2001  C  C     . VAL I  3 143 ? 67.667  77.678  121.303 1.00 16.48 ? 143  VAL A C     1 
ATOM   2002  O  O     . VAL I  3 143 ? 67.706  76.487  121.574 1.00 15.47 ? 143  VAL A O     1 
ATOM   2003  C  CB    . VAL I  3 143 ? 67.470  78.866  123.476 1.00 15.33 ? 143  VAL A CB    1 
ATOM   2004  C  CG1   . VAL I  3 143 ? 68.754  79.701  123.283 1.00 16.80 ? 143  VAL A CG1   1 
ATOM   2005  C  CG2   . VAL I  3 143 ? 66.508  79.612  124.401 1.00 16.30 ? 143  VAL A CG2   1 
ATOM   2006  N  N     . THR I  3 144 ? 68.335  78.210  120.276 1.00 15.89 ? 144  THR A N     1 
ATOM   2007  C  CA    . THR I  3 144 ? 69.196  77.389  119.427 1.00 17.00 ? 144  THR A CA    1 
ATOM   2008  C  C     . THR I  3 144 ? 70.576  78.016  119.290 1.00 15.67 ? 144  THR A C     1 
ATOM   2009  O  O     . THR I  3 144 ? 70.742  79.224  119.509 1.00 16.87 ? 144  THR A O     1 
ATOM   2010  C  CB    . THR I  3 144 ? 68.575  77.214  118.022 1.00 18.32 ? 144  THR A CB    1 
ATOM   2011  O  OG1   . THR I  3 144 ? 68.429  78.497  117.403 1.00 20.96 ? 144  THR A OG1   1 
ATOM   2012  C  CG2   . THR I  3 144 ? 67.180  76.580  118.135 1.00 18.35 ? 144  THR A CG2   1 
ATOM   2013  N  N     . ARG I  3 145 ? 71.562  77.185  118.942 1.00 16.03 ? 145  ARG A N     1 
ATOM   2014  C  CA    . ARG I  3 145 ? 72.948  77.640  118.757 1.00 16.44 ? 145  ARG A CA    1 
ATOM   2015  C  C     . ARG I  3 145 ? 73.368  77.331  117.325 1.00 18.38 ? 145  ARG A C     1 
ATOM   2016  O  O     . ARG I  3 145 ? 73.293  76.191  116.891 1.00 18.46 ? 145  ARG A O     1 
ATOM   2017  C  CB    . ARG I  3 145 ? 73.913  76.901  119.700 1.00 16.60 ? 145  ARG A CB    1 
ATOM   2018  C  CG    . ARG I  3 145 ? 75.298  77.561  119.756 1.00 16.52 ? 145  ARG A CG    1 
ATOM   2019  C  CD    . ARG I  3 145 ? 76.270  76.811  120.625 1.00 17.85 ? 145  ARG A CD    1 
ATOM   2020  N  NE    . ARG I  3 145 ? 77.576  77.469  120.630 1.00 16.93 ? 145  ARG A NE    1 
ATOM   2021  C  CZ    . ARG I  3 145 ? 78.579  77.135  121.433 1.00 17.96 ? 145  ARG A CZ    1 
ATOM   2022  N  NH1   . ARG I  3 145 ? 78.429  76.142  122.307 1.00 19.41 ? 145  ARG A NH1   1 
ATOM   2023  N  NH2   . ARG I  3 145 ? 79.738  77.796  121.372 1.00 19.99 ? 145  ARG A NH2   1 
ATOM   2024  N  N     . ASN I  3 146 ? 73.806  78.358  116.601 1.00 19.35 ? 146  ASN A N     1 
ATOM   2025  C  CA    . ASN I  3 146 ? 74.289  78.169  115.246 1.00 19.32 ? 146  ASN A CA    1 
ATOM   2026  C  C     . ASN I  3 146 ? 75.681  77.560  115.301 1.00 18.16 ? 146  ASN A C     1 
ATOM   2027  O  O     . ASN I  3 146 ? 76.401  77.708  116.285 1.00 19.43 ? 146  ASN A O     1 
ATOM   2028  C  CB    . ASN I  3 146 ? 74.328  79.515  114.522 1.00 21.03 ? 146  ASN A CB    1 
ATOM   2029  C  CG    . ASN I  3 146 ? 72.951  79.976  114.090 1.00 31.10 ? 146  ASN A CG    1 
ATOM   2030  O  OD1   . ASN I  3 146 ? 72.721  81.174  113.880 1.00 38.55 ? 146  ASN A OD1   1 
ATOM   2031  N  ND2   . ASN I  3 146 ? 72.029  79.028  113.930 1.00 30.82 ? 146  ASN A ND2   1 
ATOM   2032  N  N     . LEU I  3 147 ? 76.060  76.871  114.232 1.00 17.46 ? 147  LEU A N     1 
ATOM   2033  C  CA    . LEU I  3 147 ? 77.354  76.206  114.190 1.00 17.07 ? 147  LEU A CA    1 
ATOM   2034  C  C     . LEU I  3 147 ? 78.498  77.184  114.008 1.00 21.41 ? 147  LEU A C     1 
ATOM   2035  O  O     . LEU I  3 147 ? 78.279  78.346  113.672 1.00 22.17 ? 147  LEU A O     1 
ATOM   2036  C  CB    . LEU I  3 147 ? 77.325  75.151  113.101 1.00 15.91 ? 147  LEU A CB    1 
ATOM   2037  C  CG    . LEU I  3 147 ? 76.116  74.215  113.240 1.00 18.06 ? 147  LEU A CG    1 
ATOM   2038  C  CD1   . LEU I  3 147 ? 76.217  73.128  112.195 1.00 21.80 ? 147  LEU A CD1   1 
ATOM   2039  C  CD2   . LEU I  3 147 ? 76.061  73.571  114.647 1.00 19.09 ? 147  LEU A CD2   1 
ATOM   2040  N  N     . ILE I  3 148 ? 79.719  76.714  114.236 1.00 18.79 ? 148  ILE A N     1 
ATOM   2041  C  CA    . ILE I  3 148 ? 80.868  77.590  114.174 1.00 21.65 ? 148  ILE A CA    1 
ATOM   2042  C  C     . ILE I  3 148 ? 81.929  77.218  113.153 1.00 21.77 ? 148  ILE A C     1 
ATOM   2043  O  O     . ILE I  3 148 ? 82.100  76.046  112.781 1.00 20.42 ? 148  ILE A O     1 
ATOM   2044  C  CB    . ILE I  3 148 ? 81.508  77.698  115.552 1.00 25.84 ? 148  ILE A CB    1 
ATOM   2045  C  CG1   . ILE I  3 148 ? 82.209  76.390  115.914 1.00 22.92 ? 148  ILE A CG1   1 
ATOM   2046  C  CG2   . ILE I  3 148 ? 80.420  78.013  116.578 1.00 24.40 ? 148  ILE A CG2   1 
ATOM   2047  C  CD1   . ILE I  3 148 ? 82.874  76.377  117.284 1.00 24.33 ? 148  ILE A CD1   1 
ATOM   2048  N  N     . ALA I  3 149 ? 82.642  78.242  112.695 1.00 20.88 ? 149  ALA A N     1 
ATOM   2049  C  CA    . ALA I  3 149 ? 83.678  78.033  111.705 1.00 20.91 ? 149  ALA A CA    1 
ATOM   2050  C  C     . ALA I  3 149 ? 84.931  77.423  112.320 1.00 16.97 ? 149  ALA A C     1 
ATOM   2051  O  O     . ALA I  3 149 ? 85.216  77.567  113.530 1.00 18.13 ? 149  ALA A O     1 
ATOM   2052  C  CB    . ALA I  3 149 ? 84.024  79.367  111.043 1.00 18.36 ? 149  ALA A CB    1 
ATOM   2053  N  N     . ASP I  3 150 ? 85.714  76.755  111.484 1.00 17.27 ? 150  ASP A N     1 
ATOM   2054  C  CA    . ASP I  3 150 ? 86.964  76.184  111.956 1.00 18.51 ? 150  ASP A CA    1 
ATOM   2055  C  C     . ASP I  3 150 ? 87.881  77.290  112.501 1.00 19.36 ? 150  ASP A C     1 
ATOM   2056  O  O     . ASP I  3 150 ? 88.628  77.077  113.451 1.00 18.75 ? 150  ASP A O     1 
ATOM   2057  C  CB    . ASP I  3 150 ? 87.653  75.437  110.810 1.00 23.82 ? 150  ASP A CB    1 
ATOM   2058  C  CG    . ASP I  3 150 ? 87.023  74.092  110.532 1.00 26.57 ? 150  ASP A CG    1 
ATOM   2059  O  OD1   . ASP I  3 150 ? 86.005  73.762  111.179 1.00 27.61 ? 150  ASP A OD1   1 
ATOM   2060  O  OD2   . ASP I  3 150 ? 87.559  73.371  109.666 1.00 33.07 ? 150  ASP A OD2   1 
ATOM   2061  N  N     . ALA I  3 151 ? 87.816  78.489  111.904 1.00 19.48 ? 151  ALA A N     1 
ATOM   2062  C  CA    . ALA I  3 151 ? 88.636  79.592  112.358 1.00 17.05 ? 151  ALA A CA    1 
ATOM   2063  C  C     . ALA I  3 151 ? 88.270  80.071  113.769 1.00 14.74 ? 151  ALA A C     1 
ATOM   2064  O  O     . ALA I  3 151 ? 89.120  80.642  114.457 1.00 17.74 ? 151  ALA A O     1 
ATOM   2065  C  CB    . ALA I  3 151 ? 88.546  80.775  111.340 1.00 19.53 ? 151  ALA A CB    1 
ATOM   2066  N  N     . GLU I  3 152 ? 87.007  79.846  114.171 1.00 16.73 ? 152  GLU A N     1 
ATOM   2067  C  CA    . GLU I  3 152 ? 86.565  80.219  115.514 1.00 18.74 ? 152  GLU A CA    1 
ATOM   2068  C  C     . GLU I  3 152 ? 87.125  79.166  116.487 1.00 16.79 ? 152  GLU A C     1 
ATOM   2069  O  O     . GLU I  3 152 ? 87.662  79.495  117.561 1.00 18.53 ? 152  GLU A O     1 
ATOM   2070  C  CB    . GLU I  3 152 ? 85.027  80.255  115.586 1.00 20.23 ? 152  GLU A CB    1 
ATOM   2071  C  CG    . GLU I  3 152 ? 84.444  80.445  116.995 1.00 24.23 ? 152  GLU A CG    1 
ATOM   2072  C  CD    . GLU I  3 152 ? 84.979  81.670  117.698 1.00 34.00 ? 152  GLU A CD    1 
ATOM   2073  O  OE1   . GLU I  3 152 ? 85.447  82.612  117.001 1.00 31.95 ? 152  GLU A OE1   1 
ATOM   2074  O  OE2   . GLU I  3 152 ? 84.927  81.703  118.957 1.00 32.92 ? 152  GLU A OE2   1 
ATOM   2075  N  N     . ILE I  3 153 ? 86.999  77.905  116.111 1.00 18.15 ? 153  ILE A N     1 
ATOM   2076  C  CA    . ILE I  3 153 ? 87.542  76.832  116.947 1.00 15.94 ? 153  ILE A CA    1 
ATOM   2077  C  C     . ILE I  3 153 ? 89.039  77.069  117.088 1.00 18.19 ? 153  ILE A C     1 
ATOM   2078  O  O     . ILE I  3 153 ? 89.611  76.932  118.174 1.00 18.14 ? 153  ILE A O     1 
ATOM   2079  C  CB    . ILE I  3 153 ? 87.273  75.430  116.306 1.00 15.43 ? 153  ILE A CB    1 
ATOM   2080  C  CG1   . ILE I  3 153 ? 85.770  75.123  116.409 1.00 17.25 ? 153  ILE A CG1   1 
ATOM   2081  C  CG2   . ILE I  3 153 ? 88.079  74.303  117.053 1.00 14.27 ? 153  ILE A CG2   1 
ATOM   2082  C  CD1   . ILE I  3 153 ? 85.301  73.942  115.567 1.00 17.77 ? 153  ILE A CD1   1 
ATOM   2083  N  N     . ASN I  3 154 ? 89.675  77.469  115.986 1.00 16.57 ? 154  ASN A N     1 
ATOM   2084  C  CA    . ASN I  3 154 ? 91.114  77.690  115.968 1.00 16.16 ? 154  ASN A CA    1 
ATOM   2085  C  C     . ASN I  3 154 ? 91.530  79.116  116.301 1.00 18.54 ? 154  ASN A C     1 
ATOM   2086  O  O     . ASN I  3 154 ? 92.676  79.508  116.072 1.00 17.37 ? 154  ASN A O     1 
ATOM   2087  C  CB    . ASN I  3 154 ? 91.667  77.357  114.570 1.00 15.94 ? 154  ASN A CB    1 
ATOM   2088  C  CG    . ASN I  3 154 ? 91.572  75.885  114.217 1.00 18.91 ? 154  ASN A CG    1 
ATOM   2089  O  OD1   . ASN I  3 154 ? 91.582  75.010  115.094 1.00 16.64 ? 154  ASN A OD1   1 
ATOM   2090  N  ND2   . ASN I  3 154 ? 91.515  75.594  112.910 1.00 18.95 ? 154  ASN A ND2   1 
ATOM   2091  N  N     . ARG I  3 155 ? 90.622  79.898  116.884 1.00 17.47 ? 155  ARG A N     1 
ATOM   2092  C  CA    . ARG I  3 155 ? 90.937  81.303  117.127 1.00 18.47 ? 155  ARG A CA    1 
ATOM   2093  C  C     . ARG I  3 155 ? 92.273  81.579  117.801 1.00 19.33 ? 155  ARG A C     1 
ATOM   2094  O  O     . ARG I  3 155 ? 93.015  82.492  117.390 1.00 20.44 ? 155  ARG A O     1 
ATOM   2095  C  CB    . ARG I  3 155 ? 89.796  81.956  117.912 1.00 21.55 ? 155  ARG A CB    1 
ATOM   2096  C  CG    . ARG I  3 155 ? 90.002  83.434  118.169 1.00 23.95 ? 155  ARG A CG    1 
ATOM   2097  C  CD    . ARG I  3 155 ? 88.725  84.198  117.867 1.00 26.71 ? 155  ARG A CD    1 
ATOM   2098  N  NE    . ARG I  3 155 ? 87.587  83.769  118.674 1.00 28.56 ? 155  ARG A NE    1 
ATOM   2099  C  CZ    . ARG I  3 155 ? 87.435  84.001  119.974 1.00 29.22 ? 155  ARG A CZ    1 
ATOM   2100  N  NH1   . ARG I  3 155 ? 88.358  84.669  120.658 1.00 31.21 ? 155  ARG A NH1   1 
ATOM   2101  N  NH2   . ARG I  3 155 ? 86.339  83.567  120.589 1.00 26.74 ? 155  ARG A NH2   1 
ATOM   2102  N  N     . ASN I  3 156 ? 92.624  80.785  118.813 1.00 16.75 ? 156  ASN A N     1 
ATOM   2103  C  CA    . ASN I  3 156 ? 93.875  81.010  119.516 1.00 19.60 ? 156  ASN A CA    1 
ATOM   2104  C  C     . ASN I  3 156 ? 95.019  80.049  119.165 1.00 20.85 ? 156  ASN A C     1 
ATOM   2105  O  O     . ASN I  3 156 ? 96.198  80.401  119.279 1.00 22.41 ? 156  ASN A O     1 
ATOM   2106  C  CB    . ASN I  3 156 ? 93.626  80.986  121.042 1.00 22.73 ? 156  ASN A CB    1 
ATOM   2107  C  CG    . ASN I  3 156 ? 92.595  82.038  121.490 1.00 25.62 ? 156  ASN A CG    1 
ATOM   2108  O  OD1   . ASN I  3 156 ? 92.608  83.178  121.018 1.00 24.70 ? 156  ASN A OD1   1 
ATOM   2109  N  ND2   . ASN I  3 156 ? 91.705  81.654  122.412 1.00 27.14 ? 156  ASN A ND2   1 
ATOM   2110  N  N     . GLU I  3 157 ? 94.675  78.841  118.727 1.00 20.52 ? 157  GLU A N     1 
ATOM   2111  C  CA    . GLU I  3 157 ? 95.652  77.810  118.426 1.00 21.51 ? 157  GLU A CA    1 
ATOM   2112  C  C     . GLU I  3 157 ? 95.109  76.954  117.290 1.00 17.35 ? 157  GLU A C     1 
ATOM   2113  O  O     . GLU I  3 157 ? 93.900  76.855  117.109 1.00 19.33 ? 157  GLU A O     1 
ATOM   2114  C  CB    . GLU I  3 157 ? 95.845  76.892  119.639 1.00 25.35 ? 157  GLU A CB    1 
ATOM   2115  C  CG    . GLU I  3 157 ? 96.162  77.558  120.954 1.00 30.68 ? 157  GLU A CG    1 
ATOM   2116  C  CD    . GLU I  3 157 ? 96.212  76.554  122.094 1.00 34.43 ? 157  GLU A CD    1 
ATOM   2117  O  OE1   . GLU I  3 157 ? 97.293  75.968  122.336 1.00 31.20 ? 157  GLU A OE1   1 
ATOM   2118  O  OE2   . GLU I  3 157 ? 95.157  76.329  122.737 1.00 31.79 ? 157  GLU A OE2   1 
ATOM   2119  N  N     . PHE I  3 158 ? 96.011  76.320  116.547 1.00 18.35 ? 158  PHE A N     1 
ATOM   2120  C  CA    . PHE I  3 158 ? 95.633  75.449  115.443 1.00 19.22 ? 158  PHE A CA    1 
ATOM   2121  C  C     . PHE I  3 158 ? 95.178  74.097  116.030 1.00 18.52 ? 158  PHE A C     1 
ATOM   2122  O  O     . PHE I  3 158 ? 95.987  73.195  116.212 1.00 20.10 ? 158  PHE A O     1 
ATOM   2123  C  CB    . PHE I  3 158 ? 96.839  75.232  114.516 1.00 20.46 ? 158  PHE A CB    1 
ATOM   2124  C  CG    . PHE I  3 158 ? 96.564  74.328  113.338 1.00 18.05 ? 158  PHE A CG    1 
ATOM   2125  C  CD1   . PHE I  3 158 ? 95.337  74.340  112.687 1.00 23.40 ? 158  PHE A CD1   1 
ATOM   2126  C  CD2   . PHE I  3 158 ? 97.567  73.475  112.859 1.00 21.06 ? 158  PHE A CD2   1 
ATOM   2127  C  CE1   . PHE I  3 158 ? 95.098  73.520  111.568 1.00 24.42 ? 158  PHE A CE1   1 
ATOM   2128  C  CE2   . PHE I  3 158 ? 97.328  72.648  111.736 1.00 22.32 ? 158  PHE A CE2   1 
ATOM   2129  C  CZ    . PHE I  3 158 ? 96.096  72.678  111.102 1.00 23.13 ? 158  PHE A CZ    1 
ATOM   2130  N  N     . LEU I  3 159 ? 93.883  73.985  116.314 1.00 17.57 ? 159  LEU A N     1 
ATOM   2131  C  CA    . LEU I  3 159 ? 93.304  72.781  116.926 1.00 15.52 ? 159  LEU A CA    1 
ATOM   2132  C  C     . LEU I  3 159 ? 92.779  71.732  115.950 1.00 17.34 ? 159  LEU A C     1 
ATOM   2133  O  O     . LEU I  3 159 ? 92.956  70.535  116.178 1.00 18.33 ? 159  LEU A O     1 
ATOM   2134  C  CB    . LEU I  3 159 ? 92.167  73.171  117.883 1.00 16.64 ? 159  LEU A CB    1 
ATOM   2135  C  CG    . LEU I  3 159 ? 92.456  74.180  119.002 1.00 16.35 ? 159  LEU A CG    1 
ATOM   2136  C  CD1   . LEU I  3 159 ? 91.201  74.324  119.891 1.00 16.20 ? 159  LEU A CD1   1 
ATOM   2137  C  CD2   . LEU I  3 159 ? 93.653  73.720  119.831 1.00 17.40 ? 159  LEU A CD2   1 
ATOM   2138  N  N     . VAL I  3 160 ? 92.119  72.165  114.883 1.00 15.04 ? 160  VAL A N     1 
ATOM   2139  C  CA    . VAL I  3 160 ? 91.559  71.222  113.924 1.00 16.17 ? 160  VAL A CA    1 
ATOM   2140  C  C     . VAL I  3 160 ? 91.739  71.606  112.444 1.00 16.86 ? 160  VAL A C     1 
ATOM   2141  O  O     . VAL I  3 160 ? 91.926  72.779  112.101 1.00 18.26 ? 160  VAL A O     1 
ATOM   2142  C  CB    . VAL I  3 160 ? 90.011  71.038  114.131 1.00 17.19 ? 160  VAL A CB    1 
ATOM   2143  C  CG1   . VAL I  3 160 ? 89.708  70.582  115.582 1.00 15.97 ? 160  VAL A CG1   1 
ATOM   2144  C  CG2   . VAL I  3 160 ? 89.258  72.365  113.803 1.00 19.51 ? 160  VAL A CG2   1 
ATOM   2145  N  N     . ASP I  3 161 ? 91.722  70.577  111.595 1.00 17.48 ? 161  ASP A N     1 
ATOM   2146  C  CA    . ASP I  3 161 ? 91.713  70.772  110.144 1.00 20.21 ? 161  ASP A CA    1 
ATOM   2147  C  C     . ASP I  3 161 ? 90.608  69.841  109.635 1.00 20.36 ? 161  ASP A C     1 
ATOM   2148  O  O     . ASP I  3 161 ? 89.823  69.341  110.443 1.00 19.83 ? 161  ASP A O     1 
ATOM   2149  C  CB    . ASP I  3 161 ? 93.089  70.516  109.491 1.00 21.95 ? 161  ASP A CB    1 
ATOM   2150  C  CG    . ASP I  3 161 ? 93.532  69.071  109.516 1.00 22.11 ? 161  ASP A CG    1 
ATOM   2151  O  OD1   . ASP I  3 161 ? 92.828  68.160  110.015 1.00 19.43 ? 161  ASP A OD1   1 
ATOM   2152  O  OD2   . ASP I  3 161 ? 94.653  68.855  109.008 1.00 24.12 ? 161  ASP A OD2   1 
ATOM   2153  N  N     . GLU I  3 162 ? 90.515  69.594  108.328 1.00 18.20 ? 162  GLU A N     1 
ATOM   2154  C  CA    . GLU I  3 162 ? 89.430  68.760  107.800 1.00 22.21 ? 162  GLU A CA    1 
ATOM   2155  C  C     . GLU I  3 162 ? 89.522  67.249  108.019 1.00 19.26 ? 162  GLU A C     1 
ATOM   2156  O  O     . GLU I  3 162 ? 88.592  66.520  107.665 1.00 23.05 ? 162  GLU A O     1 
ATOM   2157  C  CB    . GLU I  3 162 ? 89.268  68.996  106.285 1.00 24.05 ? 162  GLU A CB    1 
ATOM   2158  C  CG    . GLU I  3 162 ? 90.384  68.374  105.444 1.00 28.14 ? 162  GLU A CG    1 
ATOM   2159  C  CD    . GLU I  3 162 ? 91.611  69.265  105.271 1.00 34.42 ? 162  GLU A CD    1 
ATOM   2160  O  OE1   . GLU I  3 162 ? 91.782  70.274  106.006 1.00 31.99 ? 162  GLU A OE1   1 
ATOM   2161  O  OE2   . GLU I  3 162 ? 92.429  68.941  104.381 1.00 36.34 ? 162  GLU A OE2   1 
ATOM   2162  N  N     . ASN I  3 163 ? 90.620  66.785  108.606 1.00 19.39 ? 163  ASN A N     1 
ATOM   2163  C  CA    . ASN I  3 163 ? 90.814  65.358  108.821 1.00 21.11 ? 163  ASN A CA    1 
ATOM   2164  C  C     . ASN I  3 163 ? 90.779  64.883  110.272 1.00 19.06 ? 163  ASN A C     1 
ATOM   2165  O  O     . ASN I  3 163 ? 91.149  63.744  110.543 1.00 20.05 ? 163  ASN A O     1 
ATOM   2166  C  CB    . ASN I  3 163 ? 92.142  64.923  108.201 1.00 24.89 ? 163  ASN A CB    1 
ATOM   2167  C  CG    . ASN I  3 163 ? 92.193  65.193  106.715 1.00 26.49 ? 163  ASN A CG    1 
ATOM   2168  O  OD1   . ASN I  3 163 ? 91.273  64.848  105.989 1.00 29.17 ? 163  ASN A OD1   1 
ATOM   2169  N  ND2   . ASN I  3 163 ? 93.271  65.807  106.264 1.00 30.18 ? 163  ASN A ND2   1 
ATOM   2170  N  N     . ILE I  3 164 ? 90.342  65.743  111.185 1.00 16.75 ? 164  ILE A N     1 
ATOM   2171  C  CA    . ILE I  3 164 ? 90.267  65.390  112.616 1.00 15.66 ? 164  ILE A CA    1 
ATOM   2172  C  C     . ILE I  3 164 ? 88.963  65.964  113.175 1.00 16.86 ? 164  ILE A C     1 
ATOM   2173  O  O     . ILE I  3 164 ? 88.501  66.986  112.688 1.00 17.07 ? 164  ILE A O     1 
ATOM   2174  C  CB    . ILE I  3 164 ? 91.483  65.975  113.374 1.00 14.48 ? 164  ILE A CB    1 
ATOM   2175  C  CG1   . ILE I  3 164 ? 91.521  65.473  114.825 1.00 16.28 ? 164  ILE A CG1   1 
ATOM   2176  C  CG2   . ILE I  3 164 ? 91.463  67.502  113.331 1.00 16.03 ? 164  ILE A CG2   1 
ATOM   2177  C  CD1   . ILE I  3 164 ? 92.024  64.036  114.979 1.00 18.32 ? 164  ILE A CD1   1 
ATOM   2178  N  N     . ALA I  3 165 ? 88.361  65.302  114.177 1.00 15.37 ? 165  ALA A N     1 
ATOM   2179  C  CA    . ALA I  3 165 ? 87.109  65.791  114.783 1.00 13.88 ? 165  ALA A CA    1 
ATOM   2180  C  C     . ALA I  3 165 ? 86.090  66.110  113.702 1.00 14.87 ? 165  ALA A C     1 
ATOM   2181  O  O     . ALA I  3 165 ? 85.390  67.147  113.738 1.00 16.19 ? 165  ALA A O     1 
ATOM   2182  C  CB    . ALA I  3 165 ? 87.393  67.047  115.635 1.00 16.58 ? 165  ALA A CB    1 
ATOM   2183  N  N     . THR I  3 166 ? 85.985  65.180  112.757 1.00 13.86 ? 166  THR A N     1 
ATOM   2184  C  CA    . THR I  3 166 ? 85.126  65.369  111.598 1.00 17.09 ? 166  THR A CA    1 
ATOM   2185  C  C     . THR I  3 166 ? 83.634  65.229  111.785 1.00 17.58 ? 166  THR A C     1 
ATOM   2186  O  O     . THR I  3 166 ? 82.862  65.600  110.884 1.00 18.54 ? 166  THR A O     1 
ATOM   2187  C  CB    . THR I  3 166 ? 85.573  64.451  110.436 1.00 16.10 ? 166  THR A CB    1 
ATOM   2188  O  OG1   . THR I  3 166 ? 85.335  63.086  110.781 1.00 19.71 ? 166  THR A OG1   1 
ATOM   2189  C  CG2   . THR I  3 166 ? 87.057  64.628  110.163 1.00 20.16 ? 166  THR A CG2   1 
ATOM   2190  N  N     . TYR I  3 167 ? 83.208  64.750  112.959 1.00 15.00 ? 167  TYR A N     1 
ATOM   2191  C  CA    . TYR I  3 167 ? 81.781  64.584  113.231 1.00 14.20 ? 167  TYR A CA    1 
ATOM   2192  C  C     . TYR I  3 167 ? 81.319  65.466  114.384 1.00 14.54 ? 167  TYR A C     1 
ATOM   2193  O  O     . TYR I  3 167 ? 80.168  65.339  114.832 1.00 16.22 ? 167  TYR A O     1 
ATOM   2194  C  CB    . TYR I  3 167 ? 81.472  63.109  113.562 1.00 15.40 ? 167  TYR A CB    1 
ATOM   2195  C  CG    . TYR I  3 167 ? 81.783  62.173  112.401 1.00 15.85 ? 167  TYR A CG    1 
ATOM   2196  C  CD1   . TYR I  3 167 ? 82.831  61.274  112.482 1.00 17.03 ? 167  TYR A CD1   1 
ATOM   2197  C  CD2   . TYR I  3 167 ? 81.052  62.232  111.219 1.00 20.54 ? 167  TYR A CD2   1 
ATOM   2198  C  CE1   . TYR I  3 167 ? 83.158  60.449  111.415 1.00 20.14 ? 167  TYR A CE1   1 
ATOM   2199  C  CE2   . TYR I  3 167 ? 81.371  61.409  110.145 1.00 23.81 ? 167  TYR A CE2   1 
ATOM   2200  C  CZ    . TYR I  3 167 ? 82.426  60.527  110.259 1.00 21.93 ? 167  TYR A CZ    1 
ATOM   2201  O  OH    . TYR I  3 167 ? 82.774  59.714  109.205 1.00 28.18 ? 167  TYR A OH    1 
ATOM   2202  N  N     . ALA I  3 168 ? 82.197  66.350  114.850 1.00 13.77 ? 168  ALA A N     1 
ATOM   2203  C  CA    . ALA I  3 168 ? 81.868  67.238  115.979 1.00 16.18 ? 168  ALA A CA    1 
ATOM   2204  C  C     . ALA I  3 168 ? 80.614  68.043  115.653 1.00 16.55 ? 168  ALA A C     1 
ATOM   2205  O  O     . ALA I  3 168 ? 80.523  68.704  114.615 1.00 16.04 ? 168  ALA A O     1 
ATOM   2206  C  CB    . ALA I  3 168 ? 83.024  68.183  116.273 1.00 16.10 ? 168  ALA A CB    1 
ATOM   2207  N  N     . SER I  3 169 ? 79.650  68.005  116.557 1.00 13.32 ? 169  SER A N     1 
ATOM   2208  C  CA    . SER I  3 169 ? 78.397  68.703  116.344 1.00 14.34 ? 169  SER A CA    1 
ATOM   2209  C  C     . SER I  3 169 ? 78.494  70.196  116.036 1.00 16.08 ? 169  SER A C     1 
ATOM   2210  O  O     . SER I  3 169 ? 77.693  70.718  115.259 1.00 15.63 ? 169  SER A O     1 
ATOM   2211  C  CB    . SER I  3 169 ? 77.496  68.524  117.570 1.00 19.83 ? 169  SER A CB    1 
ATOM   2212  O  OG    . SER I  3 169 ? 77.183  67.145  117.728 1.00 27.69 ? 169  SER A OG    1 
ATOM   2213  N  N     . LEU I  3 170 ? 79.458  70.877  116.645 1.00 15.34 ? 170  LEU A N     1 
ATOM   2214  C  CA    . LEU I  3 170 ? 79.569  72.319  116.436 1.00 16.68 ? 170  LEU A CA    1 
ATOM   2215  C  C     . LEU I  3 170 ? 80.123  72.724  115.106 1.00 18.44 ? 170  LEU A C     1 
ATOM   2216  O  O     . LEU I  3 170 ? 80.025  73.901  114.751 1.00 20.48 ? 170  LEU A O     1 
ATOM   2217  C  CB    . LEU I  3 170 ? 80.453  72.951  117.495 1.00 17.74 ? 170  LEU A CB    1 
ATOM   2218  C  CG    . LEU I  3 170 ? 79.790  73.067  118.857 1.00 16.98 ? 170  LEU A CG    1 
ATOM   2219  C  CD1   . LEU I  3 170 ? 80.838  73.407  119.923 1.00 18.68 ? 170  LEU A CD1   1 
ATOM   2220  C  CD2   . LEU I  3 170 ? 78.733  74.193  118.782 1.00 16.94 ? 170  LEU A CD2   1 
ATOM   2221  N  N     . ARG I  3 171 ? 80.695  71.783  114.359 1.00 17.32 ? 171  ARG A N     1 
ATOM   2222  C  CA    . ARG I  3 171 ? 81.297  72.205  113.099 1.00 19.99 ? 171  ARG A CA    1 
ATOM   2223  C  C     . ARG I  3 171 ? 80.324  72.385  111.967 1.00 20.99 ? 171  ARG A C     1 
ATOM   2224  O  O     . ARG I  3 171 ? 79.521  71.518  111.666 1.00 21.17 ? 171  ARG A O     1 
ATOM   2225  C  CB    . ARG I  3 171 ? 82.444  71.257  112.730 1.00 19.18 ? 171  ARG A CB    1 
ATOM   2226  C  CG    . ARG I  3 171 ? 83.561  71.405  113.744 1.00 20.54 ? 171  ARG A CG    1 
ATOM   2227  C  CD    . ARG I  3 171 ? 84.739  70.498  113.466 1.00 21.76 ? 171  ARG A CD    1 
ATOM   2228  N  NE    . ARG I  3 171 ? 85.569  71.028  112.379 1.00 20.16 ? 171  ARG A NE    1 
ATOM   2229  C  CZ    . ARG I  3 171 ? 86.641  70.398  111.923 1.00 23.30 ? 171  ARG A CZ    1 
ATOM   2230  N  NH1   . ARG I  3 171 ? 86.978  69.231  112.463 1.00 19.09 ? 171  ARG A NH1   1 
ATOM   2231  N  NH2   . ARG I  3 171 ? 87.379  70.938  110.959 1.00 19.63 ? 171  ARG A NH2   1 
ATOM   2232  N  N     . ALA I  3 172 ? 80.396  73.575  111.380 1.00 29.31 ? 172  ALA A N     1 
ATOM   2233  C  CA    . ALA I  3 172 ? 79.530  73.962  110.281 1.00 34.31 ? 172  ALA A CA    1 
ATOM   2234  C  C     . ALA I  3 172 ? 79.897  73.213  108.996 1.00 38.41 ? 172  ALA A C     1 
ATOM   2235  O  O     . ALA I  3 172 ? 81.070  72.919  108.751 1.00 36.90 ? 172  ALA A O     1 
ATOM   2236  C  CB    . ALA I  3 172 ? 79.640  75.473  110.066 1.00 34.63 ? 172  ALA A CB    1 
ATOM   2237  N  N     . GLY I  3 173 ? 78.887  72.881  108.196 1.00 44.98 ? 173  GLY A N     1 
ATOM   2238  C  CA    . GLY I  3 173 ? 79.141  72.206  106.932 1.00 49.15 ? 173  GLY A CA    1 
ATOM   2239  C  C     . GLY I  3 173 ? 78.999  70.699  106.742 1.00 53.56 ? 173  GLY A C     1 
ATOM   2240  O  O     . GLY I  3 173 ? 78.844  70.258  105.598 1.00 54.35 ? 173  GLY A O     1 
ATOM   2241  N  N     . ASN I  3 174 ? 79.057  69.893  107.801 1.00 54.93 ? 174  ASN A N     1 
ATOM   2242  C  CA    . ASN I  3 174 ? 78.940  68.432  107.637 1.00 58.07 ? 174  ASN A CA    1 
ATOM   2243  C  C     . ASN I  3 174 ? 77.556  68.098  107.071 1.00 58.93 ? 174  ASN A C     1 
ATOM   2244  O  O     . ASN I  3 174 ? 77.139  66.940  107.067 1.00 59.59 ? 174  ASN A O     1 
ATOM   2245  C  CB    . ASN I  3 174 ? 79.131  67.729  108.996 1.00 59.02 ? 174  ASN A CB    1 
ATOM   2246  C  CG    . ASN I  3 174 ? 79.298  66.203  108.874 1.00 60.04 ? 174  ASN A CG    1 
ATOM   2247  O  OD1   . ASN I  3 174 ? 79.295  65.642  107.773 1.00 60.04 ? 174  ASN A OD1   1 
ATOM   2248  N  ND2   . ASN I  3 174 ? 79.450  65.533  110.017 1.00 58.80 ? 174  ASN A ND2   1 
ATOM   2249  N  N     . GLY I  3 175 ? 76.874  69.127  106.566 1.00 59.16 ? 175  GLY A N     1 
ATOM   2250  C  CA    . GLY I  3 175 ? 75.518  68.979  106.063 1.00 58.08 ? 175  GLY A CA    1 
ATOM   2251  C  C     . GLY I  3 175 ? 74.706  69.158  107.336 1.00 58.10 ? 175  GLY A C     1 
ATOM   2252  O  O     . GLY I  3 175 ? 73.490  68.952  107.399 1.00 59.20 ? 175  GLY A O     1 
ATOM   2253  N  N     . ASN I  3 176 ? 75.438  69.582  108.362 1.00 54.30 ? 176  ASN A N     1 
ATOM   2254  C  CA    . ASN I  3 176 ? 74.931  69.780  109.704 1.00 50.60 ? 176  ASN A CA    1 
ATOM   2255  C  C     . ASN I  3 176 ? 74.022  70.990  109.968 1.00 45.17 ? 176  ASN A C     1 
ATOM   2256  O  O     . ASN I  3 176 ? 74.134  72.036  109.331 1.00 46.37 ? 176  ASN A O     1 
ATOM   2257  C  CB    . ASN I  3 176 ? 76.114  69.798  110.654 1.00 54.05 ? 176  ASN A CB    1 
ATOM   2258  C  CG    . ASN I  3 176 ? 75.691  69.725  112.085 1.00 59.03 ? 176  ASN A CG    1 
ATOM   2259  O  OD1   . ASN I  3 176 ? 74.544  69.378  112.379 1.00 60.03 ? 176  ASN A OD1   1 
ATOM   2260  N  ND2   . ASN I  3 176 ? 76.606  70.040  112.994 1.00 60.03 ? 176  ASN A ND2   1 
ATOM   2261  N  N     . MET I  3 177 ? 73.151  70.826  110.964 1.00 37.76 ? 177  MET A N     1 
ATOM   2262  C  CA    . MET I  3 177 ? 72.149  71.821  111.358 1.00 30.59 ? 177  MET A CA    1 
ATOM   2263  C  C     . MET I  3 177 ? 72.436  72.476  112.707 1.00 25.56 ? 177  MET A C     1 
ATOM   2264  O  O     . MET I  3 177 ? 73.305  72.019  113.448 1.00 24.89 ? 177  MET A O     1 
ATOM   2265  C  CB    . MET I  3 177 ? 70.791  71.132  111.424 1.00 30.71 ? 177  MET A CB    1 
ATOM   2266  C  CG    . MET I  3 177 ? 70.376  70.476  110.112 1.00 36.86 ? 177  MET A CG    1 
ATOM   2267  S  SD    . MET I  3 177 ? 69.459  68.942  110.398 1.00 44.00 ? 177  MET A SD    1 
ATOM   2268  C  CE    . MET I  3 177 ? 70.825  67.867  110.902 1.00 39.34 ? 177  MET A CE    1 
ATOM   2269  N  N     . PRO I  3 178 ? 71.692  73.550  113.048 1.00 21.40 ? 178  PRO A N     1 
ATOM   2270  C  CA    . PRO I  3 178 ? 71.921  74.213  114.336 1.00 20.07 ? 178  PRO A CA    1 
ATOM   2271  C  C     . PRO I  3 178 ? 71.561  73.257  115.469 1.00 16.34 ? 178  PRO A C     1 
ATOM   2272  O  O     . PRO I  3 178 ? 70.867  72.277  115.254 1.00 18.78 ? 178  PRO A O     1 
ATOM   2273  C  CB    . PRO I  3 178 ? 70.968  75.399  114.307 1.00 20.86 ? 178  PRO A CB    1 
ATOM   2274  C  CG    . PRO I  3 178 ? 70.728  75.632  112.857 1.00 27.30 ? 178  PRO A CG    1 
ATOM   2275  C  CD    . PRO I  3 178 ? 70.661  74.262  112.272 1.00 25.78 ? 178  PRO A CD    1 
ATOM   2276  N  N     . LEU I  3 179 ? 72.026  73.578  116.664 1.00 15.52 ? 179  LEU A N     1 
ATOM   2277  C  CA    . LEU I  3 179 ? 71.768  72.761  117.855 1.00 16.62 ? 179  LEU A CA    1 
ATOM   2278  C  C     . LEU I  3 179 ? 70.628  73.341  118.691 1.00 16.57 ? 179  LEU A C     1 
ATOM   2279  O  O     . LEU I  3 179 ? 70.509  74.554  118.837 1.00 18.40 ? 179  LEU A O     1 
ATOM   2280  C  CB    . LEU I  3 179 ? 73.034  72.706  118.716 1.00 18.42 ? 179  LEU A CB    1 
ATOM   2281  C  CG    . LEU I  3 179 ? 74.191  71.883  118.112 1.00 21.05 ? 179  LEU A CG    1 
ATOM   2282  C  CD1   . LEU I  3 179 ? 75.541  72.412  118.601 1.00 20.58 ? 179  LEU A CD1   1 
ATOM   2283  C  CD2   . LEU I  3 179 ? 74.001  70.404  118.507 1.00 25.28 ? 179  LEU A CD2   1 
ATOM   2284  N  N     . LEU I  3 180 ? 69.780  72.461  119.222 1.00 14.22 ? 180  LEU A N     1 
ATOM   2285  C  CA    . LEU I  3 180 ? 68.680  72.904  120.085 1.00 13.91 ? 180  LEU A CA    1 
ATOM   2286  C  C     . LEU I  3 180 ? 69.283  73.048  121.490 1.00 15.29 ? 180  LEU A C     1 
ATOM   2287  O  O     . LEU I  3 180 ? 69.756  72.070  122.073 1.00 16.39 ? 180  LEU A O     1 
ATOM   2288  C  CB    . LEU I  3 180 ? 67.530  71.883  120.070 1.00 14.36 ? 180  LEU A CB    1 
ATOM   2289  C  CG    . LEU I  3 180 ? 66.336  72.256  120.970 1.00 16.02 ? 180  LEU A CG    1 
ATOM   2290  C  CD1   . LEU I  3 180 ? 65.809  73.636  120.567 1.00 19.35 ? 180  LEU A CD1   1 
ATOM   2291  C  CD2   . LEU I  3 180 ? 65.238  71.189  120.869 1.00 18.25 ? 180  LEU A CD2   1 
ATOM   2292  N  N     . HIS I  3 181 ? 69.277  74.272  122.022 1.00 14.62 ? 181  HIS A N     1 
ATOM   2293  C  CA    . HIS I  3 181 ? 69.865  74.541  123.329 1.00 13.92 ? 181  HIS A CA    1 
ATOM   2294  C  C     . HIS I  3 181 ? 68.837  74.374  124.442 1.00 15.26 ? 181  HIS A C     1 
ATOM   2295  O  O     . HIS I  3 181 ? 69.154  73.842  125.513 1.00 13.31 ? 181  HIS A O     1 
ATOM   2296  C  CB    . HIS I  3 181 ? 70.412  75.976  123.372 1.00 15.23 ? 181  HIS A CB    1 
ATOM   2297  C  CG    . HIS I  3 181 ? 71.152  76.293  124.631 1.00 14.18 ? 181  HIS A CG    1 
ATOM   2298  N  ND1   . HIS I  3 181 ? 70.733  77.250  125.535 1.00 20.57 ? 181  HIS A ND1   1 
ATOM   2299  C  CD2   . HIS I  3 181 ? 72.283  75.757  125.137 1.00 10.73 ? 181  HIS A CD2   1 
ATOM   2300  C  CE1   . HIS I  3 181 ? 71.588  77.287  126.543 1.00 10.51 ? 181  HIS A CE1   1 
ATOM   2301  N  NE2   . HIS I  3 181 ? 72.537  76.397  126.322 1.00 17.75 ? 181  HIS A NE2   1 
ATOM   2302  N  N     . ALA I  3 182 ? 67.621  74.831  124.188 1.00 15.11 ? 182  ALA A N     1 
ATOM   2303  C  CA    . ALA I  3 182 ? 66.579  74.759  125.213 1.00 15.04 ? 182  ALA A CA    1 
ATOM   2304  C  C     . ALA I  3 182 ? 65.163  74.711  124.692 1.00 17.21 ? 182  ALA A C     1 
ATOM   2305  O  O     . ALA I  3 182 ? 64.838  75.308  123.652 1.00 15.40 ? 182  ALA A O     1 
ATOM   2306  C  CB    . ALA I  3 182 ? 66.692  75.975  126.161 1.00 15.79 ? 182  ALA A CB    1 
ATOM   2307  N  N     . SER I  3 183 ? 64.323  74.006  125.454 1.00 14.03 ? 183  SER A N     1 
ATOM   2308  C  CA    . SER I  3 183 ? 62.879  73.912  125.224 1.00 14.75 ? 183  SER A CA    1 
ATOM   2309  C  C     . SER I  3 183 ? 62.299  74.645  126.431 1.00 16.37 ? 183  SER A C     1 
ATOM   2310  O  O     . SER I  3 183 ? 62.545  74.250  127.574 1.00 16.32 ? 183  SER A O     1 
ATOM   2311  C  CB    . SER I  3 183 ? 62.386  72.470  125.275 1.00 15.58 ? 183  SER A CB    1 
ATOM   2312  O  OG    . SER I  3 183 ? 60.948  72.447  125.298 1.00 22.05 ? 183  SER A OG    1 
ATOM   2313  N  N     . ILE I  3 184 ? 61.574  75.725  126.169 1.00 15.73 ? 184  ILE A N     1 
ATOM   2314  C  CA    . ILE I  3 184 ? 60.965  76.514  127.239 1.00 15.57 ? 184  ILE A CA    1 
ATOM   2315  C  C     . ILE I  3 184 ? 59.462  76.472  127.052 1.00 18.53 ? 184  ILE A C     1 
ATOM   2316  O  O     . ILE I  3 184 ? 58.929  77.067  126.137 1.00 18.66 ? 184  ILE A O     1 
ATOM   2317  C  CB    . ILE I  3 184 ? 61.454  77.970  127.177 1.00 15.38 ? 184  ILE A CB    1 
ATOM   2318  C  CG1   . ILE I  3 184 ? 62.976  78.016  127.364 1.00 16.72 ? 184  ILE A CG1   1 
ATOM   2319  C  CG2   . ILE I  3 184 ? 60.710  78.809  128.239 1.00 17.21 ? 184  ILE A CG2   1 
ATOM   2320  C  CD1   . ILE I  3 184 ? 63.588  79.367  127.102 1.00 18.34 ? 184  ILE A CD1   1 
ATOM   2321  N  N     . SER I  3 185 ? 58.788  75.737  127.924 1.00 15.06 ? 185  SER A N     1 
ATOM   2322  C  CA    . SER I  3 185 ? 57.346  75.612  127.883 1.00 16.05 ? 185  SER A CA    1 
ATOM   2323  C  C     . SER I  3 185 ? 56.759  76.713  128.786 1.00 18.05 ? 185  SER A C     1 
ATOM   2324  O  O     . SER I  3 185 ? 57.273  76.959  129.878 1.00 19.17 ? 185  SER A O     1 
ATOM   2325  C  CB    . SER I  3 185 ? 56.965  74.229  128.411 1.00 20.48 ? 185  SER A CB    1 
ATOM   2326  O  OG    . SER I  3 185 ? 55.640  74.237  128.901 1.00 29.03 ? 185  SER A OG    1 
ATOM   2327  N  N     . CYS I  3 186 ? 55.698  77.379  128.316 1.00 15.08 ? 186  CYS A N     1 
ATOM   2328  C  CA    . CYS I  3 186 ? 55.046  78.448  129.093 1.00 16.58 ? 186  CYS A CA    1 
ATOM   2329  C  C     . CYS I  3 186 ? 53.612  78.060  129.438 1.00 15.61 ? 186  CYS A C     1 
ATOM   2330  O  O     . CYS I  3 186 ? 52.914  77.448  128.634 1.00 17.46 ? 186  CYS A O     1 
ATOM   2331  C  CB    . CYS I  3 186 ? 54.979  79.753  128.272 1.00 14.74 ? 186  CYS A CB    1 
ATOM   2332  S  SG    . CYS I  3 186 ? 56.562  80.433  127.793 1.00 18.30 ? 186  CYS A SG    1 
ATOM   2333  N  N     . LYS I  3 187 ? 53.182  78.432  130.639 1.00 16.07 ? 187  LYS A N     1 
ATOM   2334  C  CA    . LYS I  3 187 ? 51.803  78.188  131.058 1.00 17.25 ? 187  LYS A CA    1 
ATOM   2335  C  C     . LYS I  3 187 ? 51.355  79.425  131.839 1.00 16.20 ? 187  LYS A C     1 
ATOM   2336  O  O     . LYS I  3 187 ? 51.863  79.683  132.925 1.00 17.61 ? 187  LYS A O     1 
ATOM   2337  C  CB    . LYS I  3 187 ? 51.728  76.939  131.930 1.00 17.05 ? 187  LYS A CB    1 
ATOM   2338  C  CG    . LYS I  3 187 ? 52.126  75.688  131.144 1.00 15.27 ? 187  LYS A CG    1 
ATOM   2339  C  CD    . LYS I  3 187 ? 51.884  74.386  131.915 1.00 17.26 ? 187  LYS A CD    1 
ATOM   2340  C  CE    . LYS I  3 187 ? 52.136  73.157  131.021 1.00 20.67 ? 187  LYS A CE    1 
ATOM   2341  N  NZ    . LYS I  3 187 ? 51.262  73.198  129.805 1.00 22.12 ? 187  LYS A NZ    1 
ATOM   2342  N  N     . TRP I  3 188 ? 50.435  80.208  131.268 1.00 17.22 ? 188  TRP A N     1 
ATOM   2343  C  CA    . TRP I  3 188 ? 49.966  81.437  131.927 1.00 16.97 ? 188  TRP A CA    1 
ATOM   2344  C  C     . TRP I  3 188 ? 49.344  81.054  133.272 1.00 17.53 ? 188  TRP A C     1 
ATOM   2345  O  O     . TRP I  3 188 ? 49.625  81.679  134.312 1.00 17.32 ? 188  TRP A O     1 
ATOM   2346  C  CB    . TRP I  3 188 ? 48.962  82.145  131.009 1.00 19.81 ? 188  TRP A CB    1 
ATOM   2347  C  CG    . TRP I  3 188 ? 48.271  83.337  131.635 1.00 18.09 ? 188  TRP A CG    1 
ATOM   2348  C  CD1   . TRP I  3 188 ? 46.930  83.490  131.819 1.00 20.98 ? 188  TRP A CD1   1 
ATOM   2349  C  CD2   . TRP I  3 188 ? 48.892  84.517  132.172 1.00 18.08 ? 188  TRP A CD2   1 
ATOM   2350  N  NE1   . TRP I  3 188 ? 46.671  84.693  132.447 1.00 19.70 ? 188  TRP A NE1   1 
ATOM   2351  C  CE2   . TRP I  3 188 ? 47.852  85.343  132.674 1.00 17.72 ? 188  TRP A CE2   1 
ATOM   2352  C  CE3   . TRP I  3 188 ? 50.219  84.951  132.282 1.00 16.75 ? 188  TRP A CE3   1 
ATOM   2353  C  CZ2   . TRP I  3 188 ? 48.107  86.582  133.282 1.00 19.86 ? 188  TRP A CZ2   1 
ATOM   2354  C  CZ3   . TRP I  3 188 ? 50.475  86.179  132.886 1.00 18.49 ? 188  TRP A CZ3   1 
ATOM   2355  C  CH2   . TRP I  3 188 ? 49.412  86.982  133.381 1.00 23.42 ? 188  TRP A CH2   1 
ATOM   2356  N  N     . THR I  3 189 ? 48.494  80.034  133.234 1.00 16.14 ? 189  THR A N     1 
ATOM   2357  C  CA    . THR I  3 189 ? 47.900  79.472  134.459 1.00 18.02 ? 189  THR A CA    1 
ATOM   2358  C  C     . THR I  3 189 ? 47.986  77.958  134.320 1.00 18.19 ? 189  THR A C     1 
ATOM   2359  O  O     . THR I  3 189 ? 48.249  77.433  133.233 1.00 18.18 ? 189  THR A O     1 
ATOM   2360  C  CB    . THR I  3 189 ? 46.413  79.833  134.638 1.00 19.08 ? 189  THR A CB    1 
ATOM   2361  O  OG1   . THR I  3 189 ? 45.657  79.290  133.559 1.00 18.91 ? 189  THR A OG1   1 
ATOM   2362  C  CG2   . THR I  3 189 ? 46.239  81.360  134.697 1.00 22.08 ? 189  THR A CG2   1 
ATOM   2363  N  N     . ILE I  3 190 ? 47.697  77.249  135.410 1.00 15.93 ? 190  ILE A N     1 
ATOM   2364  C  CA    . ILE I  3 190 ? 47.766  75.799  135.412 1.00 17.29 ? 190  ILE A CA    1 
ATOM   2365  C  C     . ILE I  3 190 ? 46.492  75.123  135.952 1.00 18.96 ? 190  ILE A C     1 
ATOM   2366  O  O     . ILE I  3 190 ? 45.818  75.688  136.815 1.00 19.61 ? 190  ILE A O     1 
ATOM   2367  C  CB    . ILE I  3 190 ? 48.944  75.336  136.342 1.00 17.01 ? 190  ILE A CB    1 
ATOM   2368  C  CG1   . ILE I  3 190 ? 50.296  75.662  135.693 1.00 17.00 ? 190  ILE A CG1   1 
ATOM   2369  C  CG2   . ILE I  3 190 ? 48.779  73.829  136.710 1.00 20.43 ? 190  ILE A CG2   1 
ATOM   2370  C  CD1   . ILE I  3 190 ? 51.491  75.421  136.642 1.00 18.39 ? 190  ILE A CD1   1 
ATOM   2371  N  N     . ARG I  3 191 ? 46.142  73.973  135.374 1.00 18.07 ? 191  ARG A N     1 
ATOM   2372  C  CA    . ARG I  3 191 ? 45.135  73.075  135.940 1.00 17.71 ? 191  ARG A CA    1 
ATOM   2373  C  C     . ARG I  3 191 ? 46.005  71.804  135.947 1.00 17.68 ? 191  ARG A C     1 
ATOM   2374  O  O     . ARG I  3 191 ? 46.758  71.549  134.973 1.00 15.90 ? 191  ARG A O     1 
ATOM   2375  C  CB    . ARG I  3 191 ? 43.890  72.878  135.080 1.00 21.01 ? 191  ARG A CB    1 
ATOM   2376  C  CG    . ARG I  3 191 ? 42.949  74.094  135.103 1.00 17.56 ? 191  ARG A CG    1 
ATOM   2377  C  CD    . ARG I  3 191 ? 42.478  74.435  136.496 1.00 19.86 ? 191  ARG A CD    1 
ATOM   2378  N  NE    . ARG I  3 191 ? 41.534  75.553  136.451 1.00 19.68 ? 191  ARG A NE    1 
ATOM   2379  C  CZ    . ARG I  3 191 ? 41.851  76.843  136.539 1.00 20.80 ? 191  ARG A CZ    1 
ATOM   2380  N  NH1   . ARG I  3 191 ? 43.116  77.248  136.687 1.00 18.26 ? 191  ARG A NH1   1 
ATOM   2381  N  NH2   . ARG I  3 191 ? 40.879  77.752  136.463 1.00 18.78 ? 191  ARG A NH2   1 
ATOM   2382  N  N     . SER I  3 192 ? 45.927  71.009  137.015 1.00 17.74 ? 192  SER A N     1 
ATOM   2383  C  CA    . SER I  3 192 ? 46.798  69.846  137.125 1.00 16.85 ? 192  SER A CA    1 
ATOM   2384  C  C     . SER I  3 192 ? 46.690  68.802  136.017 1.00 15.81 ? 192  SER A C     1 
ATOM   2385  O  O     . SER I  3 192 ? 47.640  68.042  135.801 1.00 19.23 ? 192  SER A O     1 
ATOM   2386  C  CB    . SER I  3 192 ? 46.624  69.186  138.499 1.00 18.00 ? 192  SER A CB    1 
ATOM   2387  O  OG    . SER I  3 192 ? 45.285  68.780  138.667 1.00 18.33 ? 192  SER A OG    1 
ATOM   2388  N  N     . ASP I  3 193 ? 45.566  68.740  135.311 1.00 14.46 ? 193  ASP A N     1 
ATOM   2389  C  CA    . ASP I  3 193 ? 45.438  67.770  134.242 1.00 16.04 ? 193  ASP A CA    1 
ATOM   2390  C  C     . ASP I  3 193 ? 46.180  68.205  132.985 1.00 19.20 ? 193  ASP A C     1 
ATOM   2391  O  O     . ASP I  3 193 ? 47.050  67.474  132.451 1.00 19.28 ? 193  ASP A O     1 
ATOM   2392  C  CB    . ASP I  3 193 ? 43.956  67.498  133.899 1.00 17.29 ? 193  ASP A CB    1 
ATOM   2393  C  CG    . ASP I  3 193 ? 43.190  68.759  133.476 1.00 16.43 ? 193  ASP A CG    1 
ATOM   2394  O  OD1   . ASP I  3 193 ? 42.417  68.691  132.491 1.00 16.81 ? 193  ASP A OD1   1 
ATOM   2395  O  OD2   . ASP I  3 193 ? 43.355  69.804  134.130 1.00 17.74 ? 193  ASP A OD2   1 
ATOM   2396  N  N     . ARG I  3 194 ? 45.860  69.400  132.507 1.00 16.74 ? 194  ARG A N     1 
ATOM   2397  C  CA    . ARG I  3 194 ? 46.488  69.907  131.291 1.00 18.22 ? 194  ARG A CA    1 
ATOM   2398  C  C     . ARG I  3 194 ? 47.975  70.261  131.452 1.00 19.26 ? 194  ARG A C     1 
ATOM   2399  O  O     . ARG I  3 194 ? 48.683  70.388  130.460 1.00 23.71 ? 194  ARG A O     1 
ATOM   2400  C  CB    . ARG I  3 194 ? 45.704  71.126  130.756 1.00 19.70 ? 194  ARG A CB    1 
ATOM   2401  C  CG    . ARG I  3 194 ? 45.502  72.311  131.721 1.00 17.92 ? 194  ARG A CG    1 
ATOM   2402  C  CD    . ARG I  3 194 ? 44.691  73.446  130.966 1.00 22.27 ? 194  ARG A CD    1 
ATOM   2403  N  NE    . ARG I  3 194 ? 44.236  74.548  131.825 1.00 19.08 ? 194  ARG A NE    1 
ATOM   2404  C  CZ    . ARG I  3 194 ? 45.000  75.540  132.272 1.00 20.63 ? 194  ARG A CZ    1 
ATOM   2405  N  NH1   . ARG I  3 194 ? 46.293  75.604  131.942 1.00 20.32 ? 194  ARG A NH1   1 
ATOM   2406  N  NH2   . ARG I  3 194 ? 44.480  76.466  133.084 1.00 20.04 ? 194  ARG A NH2   1 
ATOM   2407  N  N     . ALA I  3 195 ? 48.464  70.398  132.680 1.00 15.95 ? 195  ALA A N     1 
ATOM   2408  C  CA    . ALA I  3 195 ? 49.868  70.745  132.855 1.00 17.72 ? 195  ALA A CA    1 
ATOM   2409  C  C     . ALA I  3 195 ? 50.803  69.580  132.550 1.00 15.13 ? 195  ALA A C     1 
ATOM   2410  O  O     . ALA I  3 195 ? 52.005  69.773  132.353 1.00 15.67 ? 195  ALA A O     1 
ATOM   2411  C  CB    . ALA I  3 195 ? 50.115  71.253  134.298 1.00 23.75 ? 195  ALA A CB    1 
ATOM   2412  N  N     . GLN I  3 196 ? 50.250  68.372  132.509 1.00 15.58 ? 196  GLN A N     1 
ATOM   2413  C  CA    . GLN I  3 196 ? 51.079  67.185  132.292 1.00 15.51 ? 196  GLN A CA    1 
ATOM   2414  C  C     . GLN I  3 196 ? 51.651  67.065  130.892 1.00 16.19 ? 196  GLN A C     1 
ATOM   2415  O  O     . GLN I  3 196 ? 52.542  66.230  130.657 1.00 17.16 ? 196  GLN A O     1 
ATOM   2416  C  CB    . GLN I  3 196 ? 50.301  65.905  132.655 1.00 16.97 ? 196  GLN A CB    1 
ATOM   2417  C  CG    . GLN I  3 196 ? 49.761  65.921  134.096 1.00 15.44 ? 196  GLN A CG    1 
ATOM   2418  C  CD    . GLN I  3 196 ? 50.794  66.334  135.146 1.00 20.10 ? 196  GLN A CD    1 
ATOM   2419  O  OE1   . GLN I  3 196 ? 51.924  65.851  135.157 1.00 20.18 ? 196  GLN A OE1   1 
ATOM   2420  N  NE2   . GLN I  3 196 ? 50.403  67.229  136.042 1.00 17.58 ? 196  GLN A NE2   1 
ATOM   2421  N  N     . ASN I  3 197 ? 51.158  67.859  129.950 1.00 16.33 ? 197  ASN A N     1 
ATOM   2422  C  CA    . ASN I  3 197 ? 51.751  67.785  128.612 1.00 16.37 ? 197  ASN A CA    1 
ATOM   2423  C  C     . ASN I  3 197 ? 53.210  68.278  128.644 1.00 14.29 ? 197  ASN A C     1 
ATOM   2424  O  O     . ASN I  3 197 ? 53.983  67.928  127.749 1.00 16.20 ? 197  ASN A O     1 
ATOM   2425  C  CB    . ASN I  3 197 ? 50.927  68.523  127.536 1.00 14.51 ? 197  ASN A CB    1 
ATOM   2426  C  CG    . ASN I  3 197 ? 50.844  70.053  127.725 1.00 16.59 ? 197  ASN A CG    1 
ATOM   2427  O  OD1   . ASN I  3 197 ? 51.214  70.553  128.888 1.00 21.34 ? 197  ASN A OD1   1 
ATOM   2428  N  ND2   . ASN I  3 197 ? 50.406  70.775  126.786 1.00 13.61 ? 197  ASN A ND2   1 
ATOM   2429  N  N     . ALA I  3 198 ? 53.615  69.025  129.690 1.00 14.53 ? 198  ALA A N     1 
ATOM   2430  C  CA    . ALA I  3 198 ? 55.019  69.466  129.807 1.00 15.49 ? 198  ALA A CA    1 
ATOM   2431  C  C     . ALA I  3 198 ? 55.878  68.224  130.094 1.00 17.01 ? 198  ALA A C     1 
ATOM   2432  O  O     . ALA I  3 198 ? 57.025  68.125  129.649 1.00 17.36 ? 198  ALA A O     1 
ATOM   2433  C  CB    . ALA I  3 198 ? 55.173  70.500  130.939 1.00 16.17 ? 198  ALA A CB    1 
ATOM   2434  N  N     . ARG I  3 199 ? 55.317  67.271  130.832 1.00 14.57 ? 199  ARG A N     1 
ATOM   2435  C  CA    . ARG I  3 199 ? 56.042  66.053  131.125 1.00 14.01 ? 199  ARG A CA    1 
ATOM   2436  C  C     . ARG I  3 199 ? 56.157  65.139  129.913 1.00 14.01 ? 199  ARG A C     1 
ATOM   2437  O  O     . ARG I  3 199 ? 57.227  64.546  129.675 1.00 16.79 ? 199  ARG A O     1 
ATOM   2438  C  CB    . ARG I  3 199 ? 55.385  65.267  132.285 1.00 16.68 ? 199  ARG A CB    1 
ATOM   2439  C  CG    . ARG I  3 199 ? 55.474  65.954  133.648 1.00 18.08 ? 199  ARG A CG    1 
ATOM   2440  C  CD    . ARG I  3 199 ? 54.941  65.051  134.778 1.00 18.66 ? 199  ARG A CD    1 
ATOM   2441  N  NE    . ARG I  3 199 ? 54.635  65.780  136.019 1.00 20.59 ? 199  ARG A NE    1 
ATOM   2442  C  CZ    . ARG I  3 199 ? 55.475  66.007  137.020 1.00 21.98 ? 199  ARG A CZ    1 
ATOM   2443  N  NH1   . ARG I  3 199 ? 56.733  65.571  136.975 1.00 18.85 ? 199  ARG A NH1   1 
ATOM   2444  N  NH2   . ARG I  3 199 ? 55.045  66.655  138.100 1.00 22.17 ? 199  ARG A NH2   1 
ATOM   2445  N  N     . SER I  3 200 ? 55.080  64.993  129.138 1.00 15.47 ? 200  SER A N     1 
ATOM   2446  C  CA    . SER I  3 200 ? 55.159  64.115  127.989 1.00 16.72 ? 200  SER A CA    1 
ATOM   2447  C  C     . SER I  3 200 ? 56.075  64.705  126.922 1.00 18.15 ? 200  SER A C     1 
ATOM   2448  O  O     . SER I  3 200 ? 56.838  63.964  126.273 1.00 17.39 ? 200  SER A O     1 
ATOM   2449  C  CB    . SER I  3 200 ? 53.761  63.812  127.438 1.00 18.23 ? 200  SER A CB    1 
ATOM   2450  O  OG    . SER I  3 200 ? 53.089  65.004  127.101 1.00 19.13 ? 200  SER A OG    1 
ATOM   2451  N  N     . GLU I  3 201 ? 56.047  66.030  126.768 1.00 16.36 ? 201  GLU A N     1 
ATOM   2452  C  CA    . GLU I  3 201 ? 56.929  66.656  125.785 1.00 18.87 ? 201  GLU A CA    1 
ATOM   2453  C  C     . GLU I  3 201 ? 58.378  66.501  126.251 1.00 18.09 ? 201  GLU A C     1 
ATOM   2454  O  O     . GLU I  3 201 ? 59.264  66.206  125.440 1.00 18.02 ? 201  GLU A O     1 
ATOM   2455  C  CB    . GLU I  3 201 ? 56.508  68.122  125.562 1.00 20.18 ? 201  GLU A CB    1 
ATOM   2456  C  CG    . GLU I  3 201 ? 55.282  68.172  124.624 1.00 28.47 ? 201  GLU A CG    1 
ATOM   2457  C  CD    . GLU I  3 201 ? 54.682  69.570  124.403 1.00 32.97 ? 201  GLU A CD    1 
ATOM   2458  O  OE1   . GLU I  3 201 ? 55.453  70.525  124.145 1.00 30.75 ? 201  GLU A OE1   1 
ATOM   2459  O  OE2   . GLU I  3 201 ? 53.431  69.695  124.466 1.00 36.11 ? 201  GLU A OE2   1 
ATOM   2460  N  N     . GLY I  3 202 ? 58.627  66.663  127.548 1.00 14.72 ? 202  GLY A N     1 
ATOM   2461  C  CA    . GLY I  3 202 ? 59.980  66.484  128.063 1.00 16.27 ? 202  GLY A CA    1 
ATOM   2462  C  C     . GLY I  3 202 ? 60.469  65.061  127.839 1.00 16.86 ? 202  GLY A C     1 
ATOM   2463  O  O     . GLY I  3 202 ? 61.625  64.859  127.456 1.00 16.13 ? 202  GLY A O     1 
ATOM   2464  N  N     . LEU I  3 203 ? 59.605  64.062  128.043 1.00 15.23 ? 203  LEU A N     1 
ATOM   2465  C  CA    . LEU I  3 203 ? 60.031  62.678  127.839 1.00 15.13 ? 203  LEU A CA    1 
ATOM   2466  C  C     . LEU I  3 203 ? 60.332  62.386  126.388 1.00 16.01 ? 203  LEU A C     1 
ATOM   2467  O  O     . LEU I  3 203 ? 61.227  61.581  126.093 1.00 17.98 ? 203  LEU A O     1 
ATOM   2468  C  CB    . LEU I  3 203 ? 58.997  61.685  128.380 1.00 20.03 ? 203  LEU A CB    1 
ATOM   2469  C  CG    . LEU I  3 203 ? 59.136  61.585  129.907 1.00 26.22 ? 203  LEU A CG    1 
ATOM   2470  C  CD1   . LEU I  3 203 ? 57.901  60.945  130.501 1.00 32.43 ? 203  LEU A CD1   1 
ATOM   2471  C  CD2   . LEU I  3 203 ? 60.397  60.781  130.250 1.00 31.86 ? 203  LEU A CD2   1 
ATOM   2472  N  N     . ASN I  3 204 ? 59.596  63.018  125.471 1.00 16.45 ? 204  ASN A N     1 
ATOM   2473  C  CA    . ASN I  3 204 ? 59.880  62.808  124.057 1.00 17.06 ? 204  ASN A CA    1 
ATOM   2474  C  C     . ASN I  3 204 ? 61.258  63.383  123.707 1.00 15.60 ? 204  ASN A C     1 
ATOM   2475  O  O     . ASN I  3 204 ? 62.011  62.798  122.922 1.00 16.08 ? 204  ASN A O     1 
ATOM   2476  C  CB    . ASN I  3 204 ? 58.808  63.457  123.192 1.00 19.06 ? 204  ASN A CB    1 
ATOM   2477  C  CG    . ASN I  3 204 ? 57.553  62.587  123.083 1.00 28.19 ? 204  ASN A CG    1 
ATOM   2478  O  OD1   . ASN I  3 204 ? 57.644  61.357  123.114 1.00 34.01 ? 204  ASN A OD1   1 
ATOM   2479  N  ND2   . ASN I  3 204 ? 56.390  63.216  122.938 1.00 29.76 ? 204  ASN A ND2   1 
ATOM   2480  N  N     . LEU I  3 205 ? 61.607  64.530  124.286 1.00 14.61 ? 205  LEU A N     1 
ATOM   2481  C  CA    . LEU I  3 205 ? 62.914  65.128  124.019 1.00 14.47 ? 205  LEU A CA    1 
ATOM   2482  C  C     . LEU I  3 205 ? 64.015  64.217  124.592 1.00 15.26 ? 205  LEU A C     1 
ATOM   2483  O  O     . LEU I  3 205 ? 65.100  64.060  124.007 1.00 15.10 ? 205  LEU A O     1 
ATOM   2484  C  CB    . LEU I  3 205 ? 62.994  66.519  124.676 1.00 17.26 ? 205  LEU A CB    1 
ATOM   2485  C  CG    . LEU I  3 205 ? 62.136  67.595  123.997 1.00 14.29 ? 205  LEU A CG    1 
ATOM   2486  C  CD1   . LEU I  3 205 ? 62.231  68.888  124.812 1.00 19.48 ? 205  LEU A CD1   1 
ATOM   2487  C  CD2   . LEU I  3 205 ? 62.634  67.790  122.562 1.00 22.10 ? 205  LEU A CD2   1 
ATOM   2488  N  N     . VAL I  3 206 ? 63.738  63.619  125.753 1.00 14.83 ? 206  VAL A N     1 
ATOM   2489  C  CA    . VAL I  3 206 ? 64.711  62.713  126.354 1.00 14.92 ? 206  VAL A CA    1 
ATOM   2490  C  C     . VAL I  3 206 ? 64.913  61.449  125.518 1.00 16.75 ? 206  VAL A C     1 
ATOM   2491  O  O     . VAL I  3 206 ? 66.053  61.080  125.163 1.00 15.10 ? 206  VAL A O     1 
ATOM   2492  C  CB    . VAL I  3 206 ? 64.256  62.245  127.774 1.00 13.51 ? 206  VAL A CB    1 
ATOM   2493  C  CG1   . VAL I  3 206 ? 65.139  61.081  128.260 1.00 18.61 ? 206  VAL A CG1   1 
ATOM   2494  C  CG2   . VAL I  3 206 ? 64.306  63.407  128.747 1.00 15.37 ? 206  VAL A CG2   1 
ATOM   2495  N  N     . ARG I  3 207 ? 63.797  60.790  125.214 1.00 16.16 ? 207  ARG A N     1 
ATOM   2496  C  CA    . ARG I  3 207 ? 63.821  59.517  124.502 1.00 16.03 ? 207  ARG A CA    1 
ATOM   2497  C  C     . ARG I  3 207 ? 64.343  59.504  123.087 1.00 17.28 ? 207  ARG A C     1 
ATOM   2498  O  O     . ARG I  3 207 ? 64.879  58.486  122.638 1.00 19.68 ? 207  ARG A O     1 
ATOM   2499  C  CB    . ARG I  3 207 ? 62.415  58.902  124.498 1.00 17.80 ? 207  ARG A CB    1 
ATOM   2500  C  CG    . ARG I  3 207 ? 61.966  58.475  125.887 1.00 25.63 ? 207  ARG A CG    1 
ATOM   2501  C  CD    . ARG I  3 207 ? 60.524  57.986  125.914 1.00 36.88 ? 207  ARG A CD    1 
ATOM   2502  N  NE    . ARG I  3 207 ? 60.197  57.494  127.253 1.00 45.47 ? 207  ARG A NE    1 
ATOM   2503  C  CZ    . ARG I  3 207 ? 58.972  57.189  127.673 1.00 50.32 ? 207  ARG A CZ    1 
ATOM   2504  N  NH1   . ARG I  3 207 ? 57.936  57.323  126.856 1.00 51.67 ? 207  ARG A NH1   1 
ATOM   2505  N  NH2   . ARG I  3 207 ? 58.787  56.760  128.919 1.00 49.58 ? 207  ARG A NH2   1 
ATOM   2506  N  N     . ASN I  3 208 ? 64.211  60.621  122.389 1.00 16.25 ? 208  ASN A N     1 
ATOM   2507  C  CA    . ASN I  3 208 ? 64.586  60.658  120.967 1.00 16.68 ? 208  ASN A CA    1 
ATOM   2508  C  C     . ASN I  3 208 ? 65.862  61.401  120.601 1.00 17.94 ? 208  ASN A C     1 
ATOM   2509  O  O     . ASN I  3 208 ? 66.191  61.538  119.418 1.00 20.15 ? 208  ASN A O     1 
ATOM   2510  C  CB    . ASN I  3 208 ? 63.405  61.244  120.170 1.00 17.83 ? 208  ASN A CB    1 
ATOM   2511  C  CG    . ASN I  3 208 ? 62.214  60.323  120.184 1.00 26.17 ? 208  ASN A CG    1 
ATOM   2512  O  OD1   . ASN I  3 208 ? 62.249  59.261  119.565 1.00 29.61 ? 208  ASN A OD1   1 
ATOM   2513  N  ND2   . ASN I  3 208 ? 61.175  60.685  120.933 1.00 24.75 ? 208  ASN A ND2   1 
ATOM   2514  N  N     . ARG I  3 209 ? 66.595  61.885  121.593 1.00 14.67 ? 209  ARG A N     1 
ATOM   2515  C  CA    . ARG I  3 209 ? 67.784  62.676  121.295 1.00 14.23 ? 209  ARG A CA    1 
ATOM   2516  C  C     . ARG I  3 209 ? 69.011  61.934  120.797 1.00 16.22 ? 209  ARG A C     1 
ATOM   2517  O  O     . ARG I  3 209 ? 69.245  60.775  121.143 1.00 17.32 ? 209  ARG A O     1 
ATOM   2518  C  CB    . ARG I  3 209 ? 68.251  63.438  122.540 1.00 15.10 ? 209  ARG A CB    1 
ATOM   2519  C  CG    . ARG I  3 209 ? 68.975  62.524  123.554 1.00 15.94 ? 209  ARG A CG    1 
ATOM   2520  C  CD    . ARG I  3 209 ? 69.314  63.266  124.863 1.00 14.88 ? 209  ARG A CD    1 
ATOM   2521  N  NE    . ARG I  3 209 ? 70.229  62.484  125.697 1.00 15.02 ? 209  ARG A NE    1 
ATOM   2522  C  CZ    . ARG I  3 209 ? 69.879  61.470  126.495 1.00 13.37 ? 209  ARG A CZ    1 
ATOM   2523  N  NH1   . ARG I  3 209 ? 68.609  61.083  126.614 1.00 14.69 ? 209  ARG A NH1   1 
ATOM   2524  N  NH2   . ARG I  3 209 ? 70.826  60.817  127.188 1.00 13.33 ? 209  ARG A NH2   1 
ATOM   2525  N  N     . LYS I  3 210 ? 69.786  62.641  119.980 1.00 16.76 ? 210  LYS A N     1 
ATOM   2526  C  CA    . LYS I  3 210 ? 71.092  62.153  119.534 1.00 17.83 ? 210  LYS A CA    1 
ATOM   2527  C  C     . LYS I  3 210 ? 71.955  63.347  119.905 1.00 21.36 ? 210  LYS A C     1 
ATOM   2528  O  O     . LYS I  3 210 ? 71.932  64.384  119.230 1.00 26.55 ? 210  LYS A O     1 
ATOM   2529  C  CB    . LYS I  3 210 ? 71.102  61.882  118.027 1.00 17.93 ? 210  LYS A CB    1 
ATOM   2530  C  CG    . LYS I  3 210 ? 70.223  60.710  117.667 1.00 18.58 ? 210  LYS A CG    1 
ATOM   2531  C  CD    . LYS I  3 210 ? 70.418  60.346  116.192 1.00 19.15 ? 210  LYS A CD    1 
ATOM   2532  C  CE    . LYS I  3 210 ? 69.548  59.177  115.825 1.00 23.20 ? 210  LYS A CE    1 
ATOM   2533  N  NZ    . LYS I  3 210 ? 69.770  58.801  114.370 1.00 23.03 ? 210  LYS A NZ    1 
ATOM   2534  N  N     . GLY I  3 211 ? 72.701  63.225  120.995 1.00 18.04 ? 211  GLY A N     1 
ATOM   2535  C  CA    . GLY I  3 211 ? 73.520  64.320  121.475 1.00 17.55 ? 211  GLY A CA    1 
ATOM   2536  C  C     . GLY I  3 211 ? 73.048  64.743  122.867 1.00 17.69 ? 211  GLY A C     1 
ATOM   2537  O  O     . GLY I  3 211 ? 72.212  64.038  123.441 1.00 17.41 ? 211  GLY A O     1 
ATOM   2538  N  N     . ARG I  3 212 ? 73.576  65.853  123.407 1.00 16.31 ? 212  ARG A N     1 
ATOM   2539  C  CA    . ARG I  3 212 ? 73.192  66.293  124.758 1.00 14.34 ? 212  ARG A CA    1 
ATOM   2540  C  C     . ARG I  3 212 ? 71.752  66.807  124.793 1.00 17.45 ? 212  ARG A C     1 
ATOM   2541  O  O     . ARG I  3 212 ? 71.304  67.511  123.911 1.00 18.36 ? 212  ARG A O     1 
ATOM   2542  C  CB    . ARG I  3 212 ? 74.123  67.398  125.296 1.00 14.98 ? 212  ARG A CB    1 
ATOM   2543  C  CG    . ARG I  3 212 ? 73.903  67.653  126.832 1.00 17.63 ? 212  ARG A CG    1 
ATOM   2544  C  CD    . ARG I  3 212 ? 74.764  68.788  127.426 1.00 18.49 ? 212  ARG A CD    1 
ATOM   2545  N  NE    . ARG I  3 212 ? 74.462  68.973  128.848 1.00 18.95 ? 212  ARG A NE    1 
ATOM   2546  C  CZ    . ARG I  3 212 ? 75.018  69.881  129.656 1.00 21.88 ? 212  ARG A CZ    1 
ATOM   2547  N  NH1   . ARG I  3 212 ? 75.934  70.733  129.207 1.00 20.37 ? 212  ARG A NH1   1 
ATOM   2548  N  NH2   . ARG I  3 212 ? 74.652  69.935  130.942 1.00 22.40 ? 212  ARG A NH2   1 
ATOM   2549  N  N     . LEU I  3 213 ? 71.037  66.432  125.839 1.00 14.41 ? 213  LEU A N     1 
ATOM   2550  C  CA    . LEU I  3 213 ? 69.663  66.869  126.010 1.00 13.50 ? 213  LEU A CA    1 
ATOM   2551  C  C     . LEU I  3 213 ? 69.621  68.372  126.187 1.00 14.61 ? 213  LEU A C     1 
ATOM   2552  O  O     . LEU I  3 213 ? 70.469  68.937  126.881 1.00 15.09 ? 213  LEU A O     1 
ATOM   2553  C  CB    . LEU I  3 213 ? 69.106  66.253  127.297 1.00 12.61 ? 213  LEU A CB    1 
ATOM   2554  C  CG    . LEU I  3 213 ? 67.593  66.438  127.535 1.00 13.47 ? 213  LEU A CG    1 
ATOM   2555  C  CD1   . LEU I  3 213 ? 66.807  65.640  126.511 1.00 15.11 ? 213  LEU A CD1   1 
ATOM   2556  C  CD2   . LEU I  3 213 ? 67.253  65.922  128.935 1.00 18.13 ? 213  LEU A CD2   1 
ATOM   2557  N  N     . PRO I  3 214 ? 68.662  69.045  125.529 1.00 13.91 ? 214  PRO A N     1 
ATOM   2558  C  CA    . PRO I  3 214 ? 68.521  70.505  125.674 1.00 15.18 ? 214  PRO A CA    1 
ATOM   2559  C  C     . PRO I  3 214 ? 68.047  70.801  127.103 1.00 14.67 ? 214  PRO A C     1 
ATOM   2560  O  O     . PRO I  3 214 ? 67.611  69.906  127.823 1.00 13.23 ? 214  PRO A O     1 
ATOM   2561  C  CB    . PRO I  3 214 ? 67.356  70.861  124.749 1.00 17.52 ? 214  PRO A CB    1 
ATOM   2562  C  CG    . PRO I  3 214 ? 67.295  69.726  123.730 1.00 21.71 ? 214  PRO A CG    1 
ATOM   2563  C  CD    . PRO I  3 214 ? 67.728  68.486  124.534 1.00 15.30 ? 214  PRO A CD    1 
ATOM   2564  N  N     . HIS I  3 215 ? 68.150  72.062  127.501 1.00 14.09 ? 215  HIS A N     1 
ATOM   2565  C  CA    . HIS I  3 215 ? 67.535  72.477  128.760 1.00 15.44 ? 215  HIS A CA    1 
ATOM   2566  C  C     . HIS I  3 215 ? 66.025  72.211  128.517 1.00 14.67 ? 215  HIS A C     1 
ATOM   2567  O  O     . HIS I  3 215 ? 65.517  72.420  127.415 1.00 15.02 ? 215  HIS A O     1 
ATOM   2568  C  CB    . HIS I  3 215 ? 67.708  73.982  128.971 1.00 13.84 ? 215  HIS A CB    1 
ATOM   2569  C  CG    . HIS I  3 215 ? 69.070  74.367  129.441 1.00 14.98 ? 215  HIS A CG    1 
ATOM   2570  N  ND1   . HIS I  3 215 ? 70.099  74.719  128.589 1.00 17.66 ? 215  HIS A ND1   1 
ATOM   2571  C  CD2   . HIS I  3 215 ? 69.569  74.467  130.696 1.00 13.59 ? 215  HIS A CD2   1 
ATOM   2572  C  CE1   . HIS I  3 215 ? 71.169  75.026  129.301 1.00 14.19 ? 215  HIS A CE1   1 
ATOM   2573  N  NE2   . HIS I  3 215 ? 70.873  74.880  130.582 1.00 20.31 ? 215  HIS A NE2   1 
ATOM   2574  N  N     . ILE I  3 216 ? 65.302  71.756  129.540 1.00 12.47 ? 216  ILE A N     1 
ATOM   2575  C  CA    . ILE I  3 216 ? 63.856  71.519  129.442 1.00 11.31 ? 216  ILE A CA    1 
ATOM   2576  C  C     . ILE I  3 216 ? 63.286  72.218  130.679 1.00 14.77 ? 216  ILE A C     1 
ATOM   2577  O  O     . ILE I  3 216 ? 63.454  71.731  131.815 1.00 15.10 ? 216  ILE A O     1 
ATOM   2578  C  CB    . ILE I  3 216 ? 63.502  70.005  129.474 1.00 14.15 ? 216  ILE A CB    1 
ATOM   2579  C  CG1   . ILE I  3 216 ? 64.158  69.280  128.275 1.00 16.04 ? 216  ILE A CG1   1 
ATOM   2580  C  CG2   . ILE I  3 216 ? 61.977  69.817  129.365 1.00 13.24 ? 216  ILE A CG2   1 
ATOM   2581  C  CD1   . ILE I  3 216 ? 63.962  67.788  128.281 1.00 14.99 ? 216  ILE A CD1   1 
ATOM   2582  N  N     . VAL I  3 217 ? 62.629  73.356  130.464 1.00 14.30 ? 217  VAL A N     1 
ATOM   2583  C  CA    . VAL I  3 217 ? 62.100  74.125  131.603 1.00 14.17 ? 217  VAL A CA    1 
ATOM   2584  C  C     . VAL I  3 217 ? 60.677  74.587  131.350 1.00 15.64 ? 217  VAL A C     1 
ATOM   2585  O  O     . VAL I  3 217 ? 60.184  74.541  130.226 1.00 14.05 ? 217  VAL A O     1 
ATOM   2586  C  CB    . VAL I  3 217 ? 62.978  75.364  131.870 1.00 13.30 ? 217  VAL A CB    1 
ATOM   2587  C  CG1   . VAL I  3 217 ? 64.420  74.933  132.176 1.00 16.20 ? 217  VAL A CG1   1 
ATOM   2588  C  CG2   . VAL I  3 217 ? 62.927  76.319  130.629 1.00 14.33 ? 217  VAL A CG2   1 
ATOM   2589  N  N     . VAL I  3 218 ? 60.013  75.020  132.415 1.00 13.83 ? 218  VAL A N     1 
ATOM   2590  C  CA    . VAL I  3 218 ? 58.647  75.519  132.309 1.00 14.36 ? 218  VAL A CA    1 
ATOM   2591  C  C     . VAL I  3 218 ? 58.606  76.872  133.000 1.00 16.69 ? 218  VAL A C     1 
ATOM   2592  O  O     . VAL I  3 218 ? 59.198  77.031  134.059 1.00 16.52 ? 218  VAL A O     1 
ATOM   2593  C  CB    . VAL I  3 218 ? 57.642  74.599  133.038 1.00 15.34 ? 218  VAL A CB    1 
ATOM   2594  C  CG1   . VAL I  3 218 ? 56.253  75.200  132.953 1.00 17.87 ? 218  VAL A CG1   1 
ATOM   2595  C  CG2   . VAL I  3 218 ? 57.666  73.199  132.427 1.00 14.51 ? 218  VAL A CG2   1 
ATOM   2596  N  N     . VAL I  3 219 ? 57.938  77.849  132.385 1.00 16.57 ? 219  VAL A N     1 
ATOM   2597  C  CA    . VAL I  3 219 ? 57.787  79.181  133.009 1.00 16.21 ? 219  VAL A CA    1 
ATOM   2598  C  C     . VAL I  3 219 ? 56.281  79.355  133.204 1.00 16.25 ? 219  VAL A C     1 
ATOM   2599  O  O     . VAL I  3 219 ? 55.503  79.080  132.303 1.00 15.83 ? 219  VAL A O     1 
ATOM   2600  C  CB    . VAL I  3 219 ? 58.307  80.315  132.086 1.00 16.99 ? 219  VAL A CB    1 
ATOM   2601  C  CG1   . VAL I  3 219 ? 58.002  81.703  132.737 1.00 16.92 ? 219  VAL A CG1   1 
ATOM   2602  C  CG2   . VAL I  3 219 ? 59.820  80.150  131.870 1.00 16.32 ? 219  VAL A CG2   1 
ATOM   2603  N  N     . THR I  3 220 ? 55.866  79.820  134.379 1.00 17.01 ? 220  THR A N     1 
ATOM   2604  C  CA    . THR I  3 220 ? 54.437  79.946  134.632 1.00 14.81 ? 220  THR A CA    1 
ATOM   2605  C  C     . THR I  3 220 ? 54.065  81.184  135.441 1.00 14.33 ? 220  THR A C     1 
ATOM   2606  O  O     . THR I  3 220 ? 54.887  81.717  136.192 1.00 16.98 ? 220  THR A O     1 
ATOM   2607  C  CB    . THR I  3 220 ? 53.926  78.662  135.383 1.00 16.79 ? 220  THR A CB    1 
ATOM   2608  O  OG1   . THR I  3 220 ? 52.494  78.669  135.442 1.00 17.44 ? 220  THR A OG1   1 
ATOM   2609  C  CG2   . THR I  3 220 ? 54.501  78.596  136.807 1.00 21.43 ? 220  THR A CG2   1 
ATOM   2610  N  N     . ALA I  3 221 ? 52.822  81.646  135.267 1.00 15.98 ? 221  ALA A N     1 
ATOM   2611  C  CA    . ALA I  3 221 ? 52.337  82.771  136.060 1.00 16.11 ? 221  ALA A CA    1 
ATOM   2612  C  C     . ALA I  3 221 ? 51.248  82.257  137.007 1.00 18.32 ? 221  ALA A C     1 
ATOM   2613  O  O     . ALA I  3 221 ? 50.524  83.049  137.604 1.00 17.95 ? 221  ALA A O     1 
ATOM   2614  C  CB    . ALA I  3 221 ? 51.796  83.883  135.176 1.00 18.47 ? 221  ALA A CB    1 
ATOM   2615  N  N     . GLU I  3 222 ? 51.140  80.935  137.154 1.00 17.10 ? 222  GLU A N     1 
ATOM   2616  C  CA    . GLU I  3 222 ? 50.134  80.360  138.071 1.00 16.75 ? 222  GLU A CA    1 
ATOM   2617  C  C     . GLU I  3 222 ? 50.390  80.885  139.492 1.00 17.94 ? 222  GLU A C     1 
ATOM   2618  O  O     . GLU I  3 222 ? 51.503  80.772  140.024 1.00 17.32 ? 222  GLU A O     1 
ATOM   2619  C  CB    . GLU I  3 222 ? 50.208  78.824  138.031 1.00 18.51 ? 222  GLU A CB    1 
ATOM   2620  C  CG    . GLU I  3 222 ? 49.415  78.134  139.165 1.00 18.50 ? 222  GLU A CG    1 
ATOM   2621  C  CD    . GLU I  3 222 ? 47.946  78.527  139.165 1.00 23.19 ? 222  GLU A CD    1 
ATOM   2622  O  OE1   . GLU I  3 222 ? 47.372  78.636  140.272 1.00 19.47 ? 222  GLU A OE1   1 
ATOM   2623  O  OE2   . GLU I  3 222 ? 47.358  78.715  138.072 1.00 17.68 ? 222  GLU A OE2   1 
ATOM   2624  N  N     . PRO I  3 223 ? 49.352  81.424  140.162 1.00 18.57 ? 223  PRO A N     1 
ATOM   2625  C  CA    . PRO I  3 223 ? 49.609  81.940  141.512 1.00 17.92 ? 223  PRO A CA    1 
ATOM   2626  C  C     . PRO I  3 223 ? 49.691  80.943  142.670 1.00 16.81 ? 223  PRO A C     1 
ATOM   2627  O  O     . PRO I  3 223 ? 50.351  81.214  143.681 1.00 20.32 ? 223  PRO A O     1 
ATOM   2628  C  CB    . PRO I  3 223 ? 48.460  82.948  141.719 1.00 16.24 ? 223  PRO A CB    1 
ATOM   2629  C  CG    . PRO I  3 223 ? 47.343  82.326  140.963 1.00 19.80 ? 223  PRO A CG    1 
ATOM   2630  C  CD    . PRO I  3 223 ? 48.029  81.845  139.669 1.00 19.77 ? 223  PRO A CD    1 
ATOM   2631  N  N     . THR I  3 224 ? 49.046  79.792  142.537 1.00 17.01 ? 224  THR A N     1 
ATOM   2632  C  CA    . THR I  3 224 ? 49.042  78.857  143.658 1.00 18.27 ? 224  THR A CA    1 
ATOM   2633  C  C     . THR I  3 224 ? 50.122  77.785  143.714 1.00 19.02 ? 224  THR A C     1 
ATOM   2634  O  O     . THR I  3 224 ? 50.377  77.100  142.728 1.00 21.29 ? 224  THR A O     1 
ATOM   2635  C  CB    . THR I  3 224 ? 47.666  78.143  143.793 1.00 18.60 ? 224  THR A CB    1 
ATOM   2636  O  OG1   . THR I  3 224 ? 47.426  77.281  142.670 1.00 18.75 ? 224  THR A OG1   1 
ATOM   2637  C  CG2   . THR I  3 224 ? 46.547  79.177  143.888 1.00 23.24 ? 224  THR A CG2   1 
ATOM   2638  N  N     . PRO I  3 225 ? 50.773  77.634  144.877 1.00 17.77 ? 225  PRO A N     1 
ATOM   2639  C  CA    . PRO I  3 225 ? 51.811  76.610  145.015 1.00 17.45 ? 225  PRO A CA    1 
ATOM   2640  C  C     . PRO I  3 225 ? 51.280  75.217  144.685 1.00 19.67 ? 225  PRO A C     1 
ATOM   2641  O  O     . PRO I  3 225 ? 52.000  74.394  144.107 1.00 18.55 ? 225  PRO A O     1 
ATOM   2642  C  CB    . PRO I  3 225 ? 52.225  76.724  146.496 1.00 21.16 ? 225  PRO A CB    1 
ATOM   2643  C  CG    . PRO I  3 225 ? 52.114  78.221  146.727 1.00 17.77 ? 225  PRO A CG    1 
ATOM   2644  C  CD    . PRO I  3 225 ? 50.796  78.562  146.033 1.00 19.61 ? 225  PRO A CD    1 
ATOM   2645  N  N     . SER I  3 226 ? 50.025  74.935  145.051 1.00 20.02 ? 226  SER A N     1 
ATOM   2646  C  CA    . SER I  3 226 ? 49.468  73.611  144.779 1.00 20.20 ? 226  SER A CA    1 
ATOM   2647  C  C     . SER I  3 226 ? 49.435  73.312  143.286 1.00 20.18 ? 226  SER A C     1 
ATOM   2648  O  O     . SER I  3 226 ? 49.848  72.231  142.869 1.00 19.86 ? 226  SER A O     1 
ATOM   2649  C  CB    . SER I  3 226 ? 48.053  73.461  145.379 1.00 21.85 ? 226  SER A CB    1 
ATOM   2650  O  OG    . SER I  3 226 ? 47.151  74.376  144.804 1.00 22.14 ? 226  SER A OG    1 
ATOM   2651  N  N     . ARG I  3 227 ? 48.963  74.256  142.476 1.00 19.15 ? 227  ARG A N     1 
ATOM   2652  C  CA    . ARG I  3 227 ? 48.908  74.013  141.037 1.00 18.26 ? 227  ARG A CA    1 
ATOM   2653  C  C     . ARG I  3 227 ? 50.308  74.007  140.425 1.00 16.54 ? 227  ARG A C     1 
ATOM   2654  O  O     . ARG I  3 227 ? 50.597  73.201  139.535 1.00 17.75 ? 227  ARG A O     1 
ATOM   2655  C  CB    . ARG I  3 227 ? 47.990  75.043  140.373 1.00 18.58 ? 227  ARG A CB    1 
ATOM   2656  C  CG    . ARG I  3 227 ? 46.526  74.573  140.393 1.00 19.40 ? 227  ARG A CG    1 
ATOM   2657  C  CD    . ARG I  3 227 ? 45.526  75.686  140.123 1.00 19.50 ? 227  ARG A CD    1 
ATOM   2658  N  NE    . ARG I  3 227 ? 44.203  75.105  139.960 1.00 19.49 ? 227  ARG A NE    1 
ATOM   2659  C  CZ    . ARG I  3 227 ? 43.057  75.746  140.177 1.00 23.98 ? 227  ARG A CZ    1 
ATOM   2660  N  NH1   . ARG I  3 227 ? 43.049  77.009  140.577 1.00 23.78 ? 227  ARG A NH1   1 
ATOM   2661  N  NH2   . ARG I  3 227 ? 41.913  75.121  139.974 1.00 20.21 ? 227  ARG A NH2   1 
ATOM   2662  N  N     . ILE I  3 228 ? 51.185  74.873  140.912 1.00 16.27 ? 228  ILE A N     1 
ATOM   2663  C  CA    . ILE I  3 228 ? 52.563  74.871  140.417 1.00 14.49 ? 228  ILE A CA    1 
ATOM   2664  C  C     . ILE I  3 228 ? 53.183  73.482  140.694 1.00 18.82 ? 228  ILE A C     1 
ATOM   2665  O  O     . ILE I  3 228 ? 53.899  72.915  139.834 1.00 17.66 ? 228  ILE A O     1 
ATOM   2666  C  CB    . ILE I  3 228 ? 53.417  75.929  141.155 1.00 17.59 ? 228  ILE A CB    1 
ATOM   2667  C  CG1   . ILE I  3 228 ? 52.920  77.332  140.806 1.00 17.11 ? 228  ILE A CG1   1 
ATOM   2668  C  CG2   . ILE I  3 228 ? 54.922  75.737  140.828 1.00 15.08 ? 228  ILE A CG2   1 
ATOM   2669  C  CD1   . ILE I  3 228 ? 53.436  78.378  141.769 1.00 17.78 ? 228  ILE A CD1   1 
ATOM   2670  N  N     . SER I  3 229 ? 52.903  72.925  141.877 1.00 19.16 ? 229  SER A N     1 
ATOM   2671  C  CA    . SER I  3 229 ? 53.481  71.640  142.270 1.00 18.19 ? 229  SER A CA    1 
ATOM   2672  C  C     . SER I  3 229 ? 53.119  70.473  141.354 1.00 19.56 ? 229  SER A C     1 
ATOM   2673  O  O     . SER I  3 229 ? 53.870  69.489  141.295 1.00 18.36 ? 229  SER A O     1 
ATOM   2674  C  CB    . SER I  3 229 ? 53.109  71.298  143.736 1.00 20.98 ? 229  SER A CB    1 
ATOM   2675  O  OG    . SER I  3 229 ? 51.784  70.773  143.825 1.00 22.25 ? 229  SER A OG    1 
ATOM   2676  N  N     . SER I  3 230 ? 51.998  70.588  140.632 1.00 15.64 ? 230  SER A N     1 
ATOM   2677  C  CA    . SER I  3 230 ? 51.568  69.517  139.736 1.00 18.04 ? 230  SER A CA    1 
ATOM   2678  C  C     . SER I  3 230 ? 52.564  69.305  138.580 1.00 18.00 ? 230  SER A C     1 
ATOM   2679  O  O     . SER I  3 230 ? 52.541  68.269  137.951 1.00 18.68 ? 230  SER A O     1 
ATOM   2680  C  CB    . SER I  3 230 ? 50.153  69.764  139.186 1.00 18.75 ? 230  SER A CB    1 
ATOM   2681  O  OG    . SER I  3 230 ? 50.090  70.871  138.310 1.00 21.39 ? 230  SER A OG    1 
ATOM   2682  N  N     . ILE I  3 231 ? 53.397  70.298  138.291 1.00 17.28 ? 231  ILE A N     1 
ATOM   2683  C  CA    . ILE I  3 231 ? 54.433  70.105  137.265 1.00 17.56 ? 231  ILE A CA    1 
ATOM   2684  C  C     . ILE I  3 231 ? 55.851  70.243  137.860 1.00 16.87 ? 231  ILE A C     1 
ATOM   2685  O  O     . ILE I  3 231 ? 56.791  69.622  137.361 1.00 20.21 ? 231  ILE A O     1 
ATOM   2686  C  CB    . ILE I  3 231 ? 54.216  71.080  136.058 1.00 20.10 ? 231  ILE A CB    1 
ATOM   2687  C  CG1   . ILE I  3 231 ? 55.210  70.778  134.923 1.00 28.17 ? 231  ILE A CG1   1 
ATOM   2688  C  CG2   . ILE I  3 231 ? 54.334  72.513  136.511 1.00 19.72 ? 231  ILE A CG2   1 
ATOM   2689  C  CD1   . ILE I  3 231 ? 55.000  69.407  134.242 1.00 26.22 ? 231  ILE A CD1   1 
ATOM   2690  N  N     . ALA I  3 232 ? 56.010  71.006  138.953 1.00 16.08 ? 232  ALA A N     1 
ATOM   2691  C  CA    . ALA I  3 232 ? 57.330  71.203  139.543 1.00 17.49 ? 232  ALA A CA    1 
ATOM   2692  C  C     . ALA I  3 232 ? 57.850  70.027  140.373 1.00 17.57 ? 232  ALA A C     1 
ATOM   2693  O  O     . ALA I  3 232 ? 59.054  69.728  140.371 1.00 17.51 ? 232  ALA A O     1 
ATOM   2694  C  CB    . ALA I  3 232 ? 57.338  72.472  140.409 1.00 18.72 ? 232  ALA A CB    1 
ATOM   2695  N  N     . LEU I  3 233 ? 56.965  69.346  141.094 1.00 18.29 ? 233  LEU A N     1 
ATOM   2696  C  CA    . LEU I  3 233 ? 57.449  68.224  141.912 1.00 19.75 ? 233  LEU A CA    1 
ATOM   2697  C  C     . LEU I  3 233 ? 57.858  67.024  141.075 1.00 19.96 ? 233  LEU A C     1 
ATOM   2698  O  O     . LEU I  3 233 ? 57.307  66.784  140.016 1.00 19.74 ? 233  LEU A O     1 
ATOM   2699  C  CB    . LEU I  3 233 ? 56.373  67.793  142.927 1.00 18.75 ? 233  LEU A CB    1 
ATOM   2700  C  CG    . LEU I  3 233 ? 56.018  68.816  144.003 1.00 19.73 ? 233  LEU A CG    1 
ATOM   2701  C  CD1   . LEU I  3 233 ? 54.886  68.201  144.847 1.00 22.88 ? 233  LEU A CD1   1 
ATOM   2702  C  CD2   . LEU I  3 233 ? 57.203  69.174  144.878 1.00 21.39 ? 233  LEU A CD2   1 
ATOM   2703  N  N     . GLY I  3 234 ? 58.837  66.271  141.574 1.00 20.81 ? 234  GLY A N     1 
ATOM   2704  C  CA    . GLY I  3 234 ? 59.290  65.093  140.868 1.00 22.33 ? 234  GLY A CA    1 
ATOM   2705  C  C     . GLY I  3 234 ? 60.437  65.455  139.938 1.00 21.84 ? 234  GLY A C     1 
ATOM   2706  O  O     . GLY I  3 234 ? 60.675  66.642  139.676 1.00 21.36 ? 234  GLY A O     1 
ATOM   2707  N  N     . THR I  3 235 ? 61.134  64.433  139.437 1.00 21.05 ? 235  THR A N     1 
ATOM   2708  C  CA    . THR I  3 235 ? 62.266  64.651  138.534 1.00 19.42 ? 235  THR A CA    1 
ATOM   2709  C  C     . THR I  3 235 ? 62.226  63.668  137.383 1.00 18.15 ? 235  THR A C     1 
ATOM   2710  O  O     . THR I  3 235 ? 61.523  62.655  137.436 1.00 20.40 ? 235  THR A O     1 
ATOM   2711  C  CB    . THR I  3 235 ? 63.625  64.452  139.268 1.00 18.49 ? 235  THR A CB    1 
ATOM   2712  O  OG1   . THR I  3 235 ? 63.674  63.142  139.840 1.00 21.30 ? 235  THR A OG1   1 
ATOM   2713  C  CG2   . THR I  3 235 ? 63.800  65.486  140.370 1.00 19.18 ? 235  THR A CG2   1 
ATOM   2714  N  N     . GLY I  3 236 ? 62.989  63.981  136.332 1.00 16.74 ? 236  GLY A N     1 
ATOM   2715  C  CA    . GLY I  3 236 ? 63.086  63.094  135.182 1.00 17.08 ? 236  GLY A CA    1 
ATOM   2716  C  C     . GLY I  3 236 ? 62.615  63.645  133.845 1.00 17.54 ? 236  GLY A C     1 
ATOM   2717  O  O     . GLY I  3 236 ? 63.101  63.234  132.777 1.00 17.29 ? 236  GLY A O     1 
ATOM   2718  N  N     . GLU I  3 237 ? 61.655  64.553  133.897 1.00 16.78 ? 237  GLU A N     1 
ATOM   2719  C  CA    . GLU I  3 237 ? 61.107  65.156  132.669 1.00 17.41 ? 237  GLU A CA    1 
ATOM   2720  C  C     . GLU I  3 237 ? 61.451  66.633  132.525 1.00 16.90 ? 237  GLU A C     1 
ATOM   2721  O  O     . GLU I  3 237 ? 61.910  67.073  131.468 1.00 18.97 ? 237  GLU A O     1 
ATOM   2722  C  CB    . GLU I  3 237 ? 59.581  65.047  132.660 1.00 18.16 ? 237  GLU A CB    1 
ATOM   2723  C  CG    . GLU I  3 237 ? 58.994  63.651  132.801 1.00 22.88 ? 237  GLU A CG    1 
ATOM   2724  C  CD    . GLU I  3 237 ? 58.619  63.260  134.230 1.00 27.35 ? 237  GLU A CD    1 
ATOM   2725  O  OE1   . GLU I  3 237 ? 58.384  64.126  135.117 1.00 25.74 ? 237  GLU A OE1   1 
ATOM   2726  O  OE2   . GLU I  3 237 ? 58.542  62.045  134.461 1.00 30.57 ? 237  GLU A OE2   1 
ATOM   2727  N  N     . ILE I  3 238 ? 61.226  67.375  133.606 1.00 15.94 ? 238  ILE A N     1 
ATOM   2728  C  CA    . ILE I  3 238 ? 61.416  68.812  133.690 1.00 15.51 ? 238  ILE A CA    1 
ATOM   2729  C  C     . ILE I  3 238 ? 62.636  69.172  134.529 1.00 15.52 ? 238  ILE A C     1 
ATOM   2730  O  O     . ILE I  3 238 ? 62.759  68.747  135.701 1.00 16.85 ? 238  ILE A O     1 
ATOM   2731  C  CB    . ILE I  3 238 ? 60.137  69.452  134.325 1.00 16.53 ? 238  ILE A CB    1 
ATOM   2732  C  CG1   . ILE I  3 238 ? 58.899  69.039  133.523 1.00 17.19 ? 238  ILE A CG1   1 
ATOM   2733  C  CG2   . ILE I  3 238 ? 60.266  70.964  134.426 1.00 15.57 ? 238  ILE A CG2   1 
ATOM   2734  C  CD1   . ILE I  3 238 ? 58.946  69.342  132.076 1.00 22.54 ? 238  ILE A CD1   1 
ATOM   2735  N  N     . ASP I  3 239 ? 63.541  69.964  133.957 1.00 13.70 ? 239  ASP A N     1 
ATOM   2736  C  CA    . ASP I  3 239 ? 64.746  70.359  134.694 1.00 13.00 ? 239  ASP A CA    1 
ATOM   2737  C  C     . ASP I  3 239 ? 64.420  71.207  135.924 1.00 15.29 ? 239  ASP A C     1 
ATOM   2738  O  O     . ASP I  3 239 ? 64.963  70.976  137.009 1.00 16.51 ? 239  ASP A O     1 
ATOM   2739  C  CB    . ASP I  3 239 ? 65.698  71.191  133.822 1.00 15.25 ? 239  ASP A CB    1 
ATOM   2740  C  CG    . ASP I  3 239 ? 66.246  70.423  132.617 1.00 13.68 ? 239  ASP A CG    1 
ATOM   2741  O  OD1   . ASP I  3 239 ? 65.977  69.223  132.472 1.00 15.86 ? 239  ASP A OD1   1 
ATOM   2742  O  OD2   . ASP I  3 239 ? 66.946  71.062  131.819 1.00 15.75 ? 239  ASP A OD2   1 
ATOM   2743  N  N     . CYS I  3 240 ? 63.577  72.217  135.721 1.00 16.25 ? 240  CYS A N     1 
ATOM   2744  C  CA    . CYS I  3 240 ? 63.192  73.152  136.777 1.00 15.80 ? 240  CYS A CA    1 
ATOM   2745  C  C     . CYS I  3 240 ? 62.030  74.013  136.273 1.00 19.55 ? 240  CYS A C     1 
ATOM   2746  O  O     . CYS I  3 240 ? 61.844  74.163  135.065 1.00 16.32 ? 240  CYS A O     1 
ATOM   2747  C  CB    . CYS I  3 240 ? 64.380  74.054  137.120 1.00 16.27 ? 240  CYS A CB    1 
ATOM   2748  S  SG    . CYS I  3 240 ? 64.153  74.997  138.701 1.00 17.52 ? 240  CYS A SG    1 
ATOM   2749  N  N     . VAL I  3 241 ? 61.245  74.566  137.200 1.00 14.23 ? 241  VAL A N     1 
ATOM   2750  C  CA    . VAL I  3 241 ? 60.131  75.445  136.848 1.00 13.61 ? 241  VAL A CA    1 
ATOM   2751  C  C     . VAL I  3 241 ? 60.494  76.852  137.310 1.00 15.26 ? 241  VAL A C     1 
ATOM   2752  O  O     . VAL I  3 241 ? 61.154  77.031  138.339 1.00 16.26 ? 241  VAL A O     1 
ATOM   2753  C  CB    . VAL I  3 241 ? 58.820  74.962  137.529 1.00 14.54 ? 241  VAL A CB    1 
ATOM   2754  C  CG1   . VAL I  3 241 ? 57.674  75.962  137.318 1.00 16.34 ? 241  VAL A CG1   1 
ATOM   2755  C  CG2   . VAL I  3 241 ? 58.411  73.629  136.931 1.00 15.80 ? 241  VAL A CG2   1 
ATOM   2756  N  N     . TYR I  3 242 ? 60.081  77.855  136.547 1.00 15.59 ? 242  TYR A N     1 
ATOM   2757  C  CA    . TYR I  3 242 ? 60.396  79.242  136.876 1.00 15.89 ? 242  TYR A CA    1 
ATOM   2758  C  C     . TYR I  3 242 ? 59.105  80.045  136.979 1.00 17.81 ? 242  TYR A C     1 
ATOM   2759  O  O     . TYR I  3 242 ? 58.283  79.991  136.078 1.00 18.15 ? 242  TYR A O     1 
ATOM   2760  C  CB    . TYR I  3 242 ? 61.294  79.838  135.786 1.00 15.18 ? 242  TYR A CB    1 
ATOM   2761  C  CG    . TYR I  3 242 ? 62.621  79.110  135.709 1.00 14.05 ? 242  TYR A CG    1 
ATOM   2762  C  CD1   . TYR I  3 242 ? 62.717  77.855  135.097 1.00 14.06 ? 242  TYR A CD1   1 
ATOM   2763  C  CD2   . TYR I  3 242 ? 63.767  79.659  136.292 1.00 15.96 ? 242  TYR A CD2   1 
ATOM   2764  C  CE1   . TYR I  3 242 ? 63.946  77.149  135.070 1.00 15.59 ? 242  TYR A CE1   1 
ATOM   2765  C  CE2   . TYR I  3 242 ? 64.997  78.964  136.269 1.00 16.75 ? 242  TYR A CE2   1 
ATOM   2766  C  CZ    . TYR I  3 242 ? 65.071  77.707  135.656 1.00 16.14 ? 242  TYR A CZ    1 
ATOM   2767  O  OH    . TYR I  3 242 ? 66.273  77.029  135.664 1.00 18.03 ? 242  TYR A OH    1 
ATOM   2768  N  N     . HIS I  3 243 ? 58.938  80.769  138.092 1.00 17.00 ? 243  HIS A N     1 
ATOM   2769  C  CA    . HIS I  3 243 ? 57.731  81.548  138.335 1.00 16.62 ? 243  HIS A CA    1 
ATOM   2770  C  C     . HIS I  3 243 ? 57.921  82.989  137.861 1.00 14.25 ? 243  HIS A C     1 
ATOM   2771  O  O     . HIS I  3 243 ? 58.983  83.592  138.086 1.00 17.15 ? 243  HIS A O     1 
ATOM   2772  C  CB    . HIS I  3 243 ? 57.390  81.536  139.846 1.00 17.41 ? 243  HIS A CB    1 
ATOM   2773  C  CG    . HIS I  3 243 ? 55.998  82.013  140.151 1.00 18.03 ? 243  HIS A CG    1 
ATOM   2774  N  ND1   . HIS I  3 243 ? 55.711  83.316  140.500 1.00 20.30 ? 243  HIS A ND1   1 
ATOM   2775  C  CD2   . HIS I  3 243 ? 54.807  81.373  140.072 1.00 16.38 ? 243  HIS A CD2   1 
ATOM   2776  C  CE1   . HIS I  3 243 ? 54.398  83.460  140.618 1.00 21.21 ? 243  HIS A CE1   1 
ATOM   2777  N  NE2   . HIS I  3 243 ? 53.825  82.295  140.364 1.00 17.58 ? 243  HIS A NE2   1 
ATOM   2778  N  N     . PHE I  3 244 ? 56.880  83.543  137.241 1.00 15.28 ? 244  PHE A N     1 
ATOM   2779  C  CA    . PHE I  3 244 ? 56.954  84.897  136.710 1.00 18.46 ? 244  PHE A CA    1 
ATOM   2780  C  C     . PHE I  3 244 ? 57.137  85.996  137.753 1.00 18.42 ? 244  PHE A C     1 
ATOM   2781  O  O     . PHE I  3 244 ? 57.567  87.103  137.417 1.00 19.10 ? 244  PHE A O     1 
ATOM   2782  C  CB    . PHE I  3 244 ? 55.721  85.206  135.832 1.00 16.79 ? 244  PHE A CB    1 
ATOM   2783  C  CG    . PHE I  3 244 ? 54.582  85.880  136.565 1.00 20.49 ? 244  PHE A CG    1 
ATOM   2784  C  CD1   . PHE I  3 244 ? 54.125  87.129  136.147 1.00 20.71 ? 244  PHE A CD1   1 
ATOM   2785  C  CD2   . PHE I  3 244 ? 53.935  85.251  137.642 1.00 18.91 ? 244  PHE A CD2   1 
ATOM   2786  C  CE1   . PHE I  3 244 ? 53.034  87.740  136.776 1.00 20.68 ? 244  PHE A CE1   1 
ATOM   2787  C  CE2   . PHE I  3 244 ? 52.840  85.866  138.275 1.00 21.01 ? 244  PHE A CE2   1 
ATOM   2788  C  CZ    . PHE I  3 244 ? 52.397  87.103  137.837 1.00 19.05 ? 244  PHE A CZ    1 
ATOM   2789  N  N     . ALA I  3 245 ? 56.847  85.686  139.016 1.00 17.03 ? 245  ALA A N     1 
ATOM   2790  C  CA    . ALA I  3 245 ? 56.979  86.691  140.077 1.00 17.28 ? 245  ALA A CA    1 
ATOM   2791  C  C     . ALA I  3 245 ? 57.187  85.981  141.403 1.00 21.06 ? 245  ALA A C     1 
ATOM   2792  O  O     . ALA I  3 245 ? 56.392  86.095  142.339 1.00 21.25 ? 245  ALA A O     1 
ATOM   2793  C  CB    . ALA I  3 245 ? 55.708  87.555  140.117 1.00 20.38 ? 245  ALA A CB    1 
ATOM   2794  N  N     . LEU I  3 246 ? 58.297  85.275  141.505 1.00 17.50 ? 246  LEU A N     1 
ATOM   2795  C  CA    . LEU I  3 246 ? 58.545  84.488  142.692 1.00 18.15 ? 246  LEU A CA    1 
ATOM   2796  C  C     . LEU I  3 246 ? 58.653  85.260  144.003 1.00 20.68 ? 246  LEU A C     1 
ATOM   2797  O  O     . LEU I  3 246 ? 58.097  84.822  145.012 1.00 21.60 ? 246  LEU A O     1 
ATOM   2798  C  CB    . LEU I  3 246 ? 59.812  83.640  142.505 1.00 17.90 ? 246  LEU A CB    1 
ATOM   2799  C  CG    . LEU I  3 246 ? 59.929  82.517  143.551 1.00 20.92 ? 246  LEU A CG    1 
ATOM   2800  C  CD1   . LEU I  3 246 ? 59.089  81.308  143.142 1.00 22.02 ? 246  LEU A CD1   1 
ATOM   2801  C  CD2   . LEU I  3 246 ? 61.368  82.112  143.704 1.00 20.61 ? 246  LEU A CD2   1 
ATOM   2802  N  N     . TYR I  3 247 ? 59.379  86.376  143.978 1.00 20.35 ? 247  TYR A N     1 
ATOM   2803  C  CA    . TYR I  3 247 ? 59.583  87.190  145.176 1.00 22.72 ? 247  TYR A CA    1 
ATOM   2804  C  C     . TYR I  3 247 ? 58.254  87.697  145.718 1.00 24.37 ? 247  TYR A C     1 
ATOM   2805  O  O     . TYR I  3 247 ? 58.026  87.684  146.935 1.00 23.71 ? 247  TYR A O     1 
ATOM   2806  C  CB    . TYR I  3 247 ? 60.491  88.375  144.856 1.00 22.31 ? 247  TYR A CB    1 
ATOM   2807  C  CG    . TYR I  3 247 ? 61.792  87.979  144.170 1.00 22.00 ? 247  TYR A CG    1 
ATOM   2808  C  CD1   . TYR I  3 247 ? 62.402  88.844  143.257 1.00 23.28 ? 247  TYR A CD1   1 
ATOM   2809  C  CD2   . TYR I  3 247 ? 62.377  86.733  144.405 1.00 24.23 ? 247  TYR A CD2   1 
ATOM   2810  C  CE1   . TYR I  3 247 ? 63.562  88.473  142.580 1.00 24.02 ? 247  TYR A CE1   1 
ATOM   2811  C  CE2   . TYR I  3 247 ? 63.547  86.345  143.732 1.00 23.73 ? 247  TYR A CE2   1 
ATOM   2812  C  CZ    . TYR I  3 247 ? 64.125  87.223  142.818 1.00 24.35 ? 247  TYR A CZ    1 
ATOM   2813  O  OH    . TYR I  3 247 ? 65.247  86.849  142.109 1.00 23.66 ? 247  TYR A OH    1 
ATOM   2814  N  N     . GLU I  3 248 ? 57.390  88.137  144.814 1.00 23.47 ? 248  GLU A N     1 
ATOM   2815  C  CA    . GLU I  3 248 ? 56.083  88.658  145.190 1.00 24.06 ? 248  GLU A CA    1 
ATOM   2816  C  C     . GLU I  3 248 ? 55.183  87.544  145.723 1.00 23.80 ? 248  GLU A C     1 
ATOM   2817  O  O     . GLU I  3 248 ? 54.435  87.754  146.692 1.00 20.38 ? 248  GLU A O     1 
ATOM   2818  C  CB    . GLU I  3 248 ? 55.444  89.365  144.000 1.00 19.30 ? 248  GLU A CB    1 
ATOM   2819  C  CG    . GLU I  3 248 ? 56.232  90.582  143.506 1.00 22.04 ? 248  GLU A CG    1 
ATOM   2820  C  CD    . GLU I  3 248 ? 57.478  90.245  142.675 1.00 26.05 ? 248  GLU A CD    1 
ATOM   2821  O  OE1   . GLU I  3 248 ? 57.748  89.047  142.407 1.00 22.88 ? 248  GLU A OE1   1 
ATOM   2822  O  OE2   . GLU I  3 248 ? 58.185  91.202  142.284 1.00 24.84 ? 248  GLU A OE2   1 
ATOM   2823  N  N     . LEU I  3 249 ? 55.251  86.358  145.106 1.00 20.60 ? 249  LEU A N     1 
ATOM   2824  C  CA    . LEU I  3 249 ? 54.483  85.213  145.575 1.00 19.00 ? 249  LEU A CA    1 
ATOM   2825  C  C     . LEU I  3 249 ? 54.916  84.886  147.007 1.00 23.60 ? 249  LEU A C     1 
ATOM   2826  O  O     . LEU I  3 249 ? 54.076  84.661  147.884 1.00 25.05 ? 249  LEU A O     1 
ATOM   2827  C  CB    . LEU I  3 249 ? 54.737  83.980  144.692 1.00 20.19 ? 249  LEU A CB    1 
ATOM   2828  C  CG    . LEU I  3 249 ? 54.202  82.625  145.173 1.00 17.62 ? 249  LEU A CG    1 
ATOM   2829  C  CD1   . LEU I  3 249 ? 52.695  82.654  145.462 1.00 18.24 ? 249  LEU A CD1   1 
ATOM   2830  C  CD2   . LEU I  3 249 ? 54.480  81.611  144.055 1.00 22.14 ? 249  LEU A CD2   1 
ATOM   2831  N  N     . GLU I  3 250 ? 56.227  84.856  147.236 1.00 21.46 ? 250  GLU A N     1 
ATOM   2832  C  CA    . GLU I  3 250 ? 56.753  84.546  148.567 1.00 22.38 ? 250  GLU A CA    1 
ATOM   2833  C  C     . GLU I  3 250 ? 56.288  85.584  149.587 1.00 24.33 ? 250  GLU A C     1 
ATOM   2834  O  O     . GLU I  3 250 ? 55.887  85.224  150.700 1.00 24.25 ? 250  GLU A O     1 
ATOM   2835  C  CB    . GLU I  3 250 ? 58.286  84.505  148.554 1.00 22.02 ? 250  GLU A CB    1 
ATOM   2836  C  CG    . GLU I  3 250 ? 58.903  84.102  149.887 1.00 25.55 ? 250  GLU A CG    1 
ATOM   2837  C  CD    . GLU I  3 250 ? 60.432  84.132  149.868 1.00 29.15 ? 250  GLU A CD    1 
ATOM   2838  O  OE1   . GLU I  3 250 ? 61.024  84.965  149.145 1.00 33.22 ? 250  GLU A OE1   1 
ATOM   2839  O  OE2   . GLU I  3 250 ? 61.042  83.325  150.597 1.00 34.37 ? 250  GLU A OE2   1 
ATOM   2840  N  N     . GLN I  3 251 ? 56.332  86.855  149.202 1.00 23.82 ? 251  GLN A N     1 
ATOM   2841  C  CA    . GLN I  3 251 ? 55.919  87.935  150.118 1.00 24.63 ? 251  GLN A CA    1 
ATOM   2842  C  C     . GLN I  3 251 ? 54.436  87.829  150.479 1.00 24.82 ? 251  GLN A C     1 
ATOM   2843  O  O     . GLN I  3 251 ? 54.052  88.014  151.655 1.00 24.97 ? 251  GLN A O     1 
ATOM   2844  C  CB    . GLN I  3 251 ? 56.202  89.301  149.482 1.00 26.57 ? 251  GLN A CB    1 
ATOM   2845  C  CG    . GLN I  3 251 ? 56.106  90.493  150.451 1.00 38.39 ? 251  GLN A CG    1 
ATOM   2846  C  CD    . GLN I  3 251 ? 56.540  91.804  149.797 1.00 45.59 ? 251  GLN A CD    1 
ATOM   2847  O  OE1   . GLN I  3 251 ? 57.580  91.866  149.132 1.00 47.44 ? 251  GLN A OE1   1 
ATOM   2848  N  NE2   . GLN I  3 251 ? 55.745  92.854  149.982 1.00 49.80 ? 251  GLN A NE2   1 
ATOM   2849  N  N     . ILE I  3 252 ? 53.592  87.537  149.488 1.00 20.83 ? 252  ILE A N     1 
ATOM   2850  C  CA    . ILE I  3 252 ? 52.161  87.444  149.782 1.00 23.58 ? 252  ILE A CA    1 
ATOM   2851  C  C     . ILE I  3 252 ? 51.849  86.251  150.663 1.00 24.68 ? 252  ILE A C     1 
ATOM   2852  O  O     . ILE I  3 252 ? 51.067  86.369  151.614 1.00 22.03 ? 252  ILE A O     1 
ATOM   2853  C  CB    . ILE I  3 252 ? 51.304  87.408  148.499 1.00 23.26 ? 252  ILE A CB    1 
ATOM   2854  C  CG1   . ILE I  3 252 ? 51.517  88.718  147.735 1.00 30.21 ? 252  ILE A CG1   1 
ATOM   2855  C  CG2   . ILE I  3 252 ? 49.804  87.287  148.841 1.00 25.56 ? 252  ILE A CG2   1 
ATOM   2856  C  CD1   . ILE I  3 252 ? 51.235  89.977  148.593 1.00 28.71 ? 252  ILE A CD1   1 
ATOM   2857  N  N     . LEU I  3 253 ? 52.462  85.101  150.374 1.00 22.61 ? 253  LEU A N     1 
ATOM   2858  C  CA    . LEU I  3 253 ? 52.231  83.928  151.206 1.00 20.74 ? 253  LEU A CA    1 
ATOM   2859  C  C     . LEU I  3 253 ? 52.640  84.237  152.649 1.00 20.31 ? 253  LEU A C     1 
ATOM   2860  O  O     . LEU I  3 253 ? 51.933  83.866  153.587 1.00 25.26 ? 253  LEU A O     1 
ATOM   2861  C  CB    . LEU I  3 253 ? 53.037  82.732  150.699 1.00 20.40 ? 253  LEU A CB    1 
ATOM   2862  C  CG    . LEU I  3 253 ? 52.623  82.238  149.302 1.00 20.58 ? 253  LEU A CG    1 
ATOM   2863  C  CD1   . LEU I  3 253 ? 53.621  81.180  148.833 1.00 19.77 ? 253  LEU A CD1   1 
ATOM   2864  C  CD2   . LEU I  3 253 ? 51.230  81.647  149.314 1.00 19.22 ? 253  LEU A CD2   1 
ATOM   2865  N  N     . GLN I  3 254 ? 53.775  84.903  152.826 1.00 21.48 ? 254  GLN A N     1 
ATOM   2866  C  CA    . GLN I  3 254 ? 54.240  85.239  154.174 1.00 22.68 ? 254  GLN A CA    1 
ATOM   2867  C  C     . GLN I  3 254 ? 53.293  86.213  154.849 1.00 23.10 ? 254  GLN A C     1 
ATOM   2868  O  O     . GLN I  3 254 ? 52.935  86.029  156.019 1.00 25.26 ? 254  GLN A O     1 
ATOM   2869  C  CB    . GLN I  3 254 ? 55.643  85.836  154.114 1.00 23.43 ? 254  GLN A CB    1 
ATOM   2870  C  CG    . GLN I  3 254 ? 56.728  84.816  153.752 1.00 27.87 ? 254  GLN A CG    1 
ATOM   2871  C  CD    . GLN I  3 254 ? 57.159  83.963  154.950 1.00 37.95 ? 254  GLN A CD    1 
ATOM   2872  O  OE1   . GLN I  3 254 ? 56.501  83.953  156.000 1.00 38.33 ? 254  GLN A OE1   1 
ATOM   2873  N  NE2   . GLN I  3 254 ? 58.268  83.241  154.793 1.00 38.90 ? 254  GLN A NE2   1 
ATOM   2874  N  N     . SER I  3 255 ? 52.884  87.245  154.121 1.00 23.29 ? 255  SER A N     1 
ATOM   2875  C  CA    . SER I  3 255 ? 51.981  88.263  154.667 1.00 25.19 ? 255  SER A CA    1 
ATOM   2876  C  C     . SER I  3 255 ? 50.661  87.691  155.152 1.00 26.66 ? 255  SER A C     1 
ATOM   2877  O  O     . SER I  3 255 ? 50.211  88.025  156.257 1.00 30.70 ? 255  SER A O     1 
ATOM   2878  C  CB    . SER I  3 255 ? 51.702  89.339  153.616 1.00 23.61 ? 255  SER A CB    1 
ATOM   2879  O  OG    . SER I  3 255 ? 52.858  90.126  153.420 1.00 30.77 ? 255  SER A OG    1 
ATOM   2880  N  N     . LEU I  3 256 ? 50.029  86.860  154.325 1.00 24.04 ? 256  LEU A N     1 
ATOM   2881  C  CA    . LEU I  3 256 ? 48.738  86.241  154.663 1.00 23.78 ? 256  LEU A CA    1 
ATOM   2882  C  C     . LEU I  3 256 ? 48.828  85.016  155.573 1.00 26.25 ? 256  LEU A C     1 
ATOM   2883  O  O     . LEU I  3 256 ? 47.803  84.465  155.980 1.00 26.31 ? 256  LEU A O     1 
ATOM   2884  C  CB    . LEU I  3 256 ? 47.985  85.850  153.387 1.00 25.03 ? 256  LEU A CB    1 
ATOM   2885  C  CG    . LEU I  3 256 ? 47.779  87.001  152.394 1.00 27.08 ? 256  LEU A CG    1 
ATOM   2886  C  CD1   . LEU I  3 256 ? 46.964  86.523  151.204 1.00 26.70 ? 256  LEU A CD1   1 
ATOM   2887  C  CD2   . LEU I  3 256 ? 47.064  88.157  153.099 1.00 30.06 ? 256  LEU A CD2   1 
ATOM   2888  N  N     . ASN I  3 257 ? 50.043  84.588  155.896 1.00 25.57 ? 257  ASN A N     1 
ATOM   2889  C  CA    . ASN I  3 257 ? 50.242  83.419  156.743 1.00 27.74 ? 257  ASN A CA    1 
ATOM   2890  C  C     . ASN I  3 257 ? 49.494  82.180  156.232 1.00 29.85 ? 257  ASN A C     1 
ATOM   2891  O  O     . ASN I  3 257 ? 48.804  81.499  156.996 1.00 30.16 ? 257  ASN A O     1 
ATOM   2892  C  CB    . ASN I  3 257 ? 49.843  83.716  158.212 1.00 30.44 ? 257  ASN A CB    1 
ATOM   2893  C  CG    . ASN I  3 257 ? 50.774  84.721  158.889 1.00 35.16 ? 257  ASN A CG    1 
ATOM   2894  O  OD1   . ASN I  3 257 ? 52.000  84.611  158.796 1.00 40.95 ? 257  ASN A OD1   1 
ATOM   2895  N  ND2   . ASN I  3 257 ? 50.197  85.699  159.587 1.00 29.03 ? 257  ASN A ND2   1 
ATOM   2896  N  N     . TYR I  3 258 ? 49.621  81.889  154.933 1.00 28.10 ? 258  TYR A N     1 
ATOM   2897  C  CA    . TYR I  3 258 ? 49.000  80.695  154.351 1.00 26.96 ? 258  TYR A CA    1 
ATOM   2898  C  C     . TYR I  3 258 ? 50.077  79.633  154.567 1.00 31.97 ? 258  TYR A C     1 
ATOM   2899  O  O     . TYR I  3 258 ? 50.889  79.346  153.683 1.00 28.50 ? 258  TYR A O     1 
ATOM   2900  C  CB    . TYR I  3 258 ? 48.747  80.865  152.849 1.00 29.75 ? 258  TYR A CB    1 
ATOM   2901  C  CG    . TYR I  3 258 ? 47.576  81.750  152.472 1.00 29.43 ? 258  TYR A CG    1 
ATOM   2902  C  CD1   . TYR I  3 258 ? 47.314  82.031  151.131 1.00 28.53 ? 258  TYR A CD1   1 
ATOM   2903  C  CD2   . TYR I  3 258 ? 46.707  82.270  153.436 1.00 29.47 ? 258  TYR A CD2   1 
ATOM   2904  C  CE1   . TYR I  3 258 ? 46.226  82.796  150.746 1.00 29.27 ? 258  TYR A CE1   1 
ATOM   2905  C  CE2   . TYR I  3 258 ? 45.596  83.047  153.057 1.00 29.01 ? 258  TYR A CE2   1 
ATOM   2906  C  CZ    . TYR I  3 258 ? 45.367  83.296  151.707 1.00 30.16 ? 258  TYR A CZ    1 
ATOM   2907  O  OH    . TYR I  3 258 ? 44.267  84.010  151.290 1.00 31.06 ? 258  TYR A OH    1 
ATOM   2908  N  N     . GLU I  3 259 ? 50.084  79.067  155.767 1.00 29.16 ? 259  GLU A N     1 
ATOM   2909  C  CA    . GLU I  3 259 ? 51.078  78.091  156.173 1.00 30.89 ? 259  GLU A CA    1 
ATOM   2910  C  C     . GLU I  3 259 ? 51.296  76.864  155.290 1.00 28.25 ? 259  GLU A C     1 
ATOM   2911  O  O     . GLU I  3 259 ? 52.444  76.502  155.038 1.00 27.70 ? 259  GLU A O     1 
ATOM   2912  C  CB    . GLU I  3 259 ? 50.786  77.637  157.602 1.00 34.53 ? 259  GLU A CB    1 
ATOM   2913  C  CG    . GLU I  3 259 ? 50.697  78.789  158.608 1.00 44.03 ? 259  GLU A CG    1 
ATOM   2914  C  CD    . GLU I  3 259 ? 51.978  79.598  158.705 1.00 50.92 ? 259  GLU A CD    1 
ATOM   2915  O  OE1   . GLU I  3 259 ? 52.985  79.214  158.064 1.00 58.02 ? 259  GLU A OE1   1 
ATOM   2916  O  OE2   . GLU I  3 259 ? 51.983  80.619  159.433 1.00 57.71 ? 259  GLU A OE2   1 
ATOM   2917  N  N     . ASP I  3 260 ? 50.226  76.207  154.851 1.00 25.77 ? 260  ASP A N     1 
ATOM   2918  C  CA    . ASP I  3 260 ? 50.405  75.024  154.013 1.00 28.20 ? 260  ASP A CA    1 
ATOM   2919  C  C     . ASP I  3 260 ? 51.022  75.427  152.665 1.00 28.61 ? 260  ASP A C     1 
ATOM   2920  O  O     . ASP I  3 260 ? 51.988  74.797  152.192 1.00 25.85 ? 260  ASP A O     1 
ATOM   2921  C  CB    . ASP I  3 260 ? 49.074  74.296  153.799 1.00 30.21 ? 260  ASP A CB    1 
ATOM   2922  C  CG    . ASP I  3 260 ? 48.617  73.519  155.049 1.00 39.76 ? 260  ASP A CG    1 
ATOM   2923  O  OD1   . ASP I  3 260 ? 49.362  73.488  156.062 1.00 39.38 ? 260  ASP A OD1   1 
ATOM   2924  O  OD2   . ASP I  3 260 ? 47.513  72.934  155.015 1.00 39.29 ? 260  ASP A OD2   1 
ATOM   2925  N  N     . ALA I  3 261 ? 50.477  76.474  152.050 1.00 23.81 ? 261  ALA A N     1 
ATOM   2926  C  CA    . ALA I  3 261 ? 51.011  76.927  150.763 1.00 23.32 ? 261  ALA A CA    1 
ATOM   2927  C  C     . ALA I  3 261 ? 52.473  77.341  150.937 1.00 26.84 ? 261  ALA A C     1 
ATOM   2928  O  O     . ALA I  3 261 ? 53.309  77.109  150.060 1.00 24.29 ? 261  ALA A O     1 
ATOM   2929  C  CB    . ALA I  3 261 ? 50.183  78.083  150.215 1.00 21.39 ? 261  ALA A CB    1 
ATOM   2930  N  N     . LEU I  3 262 ? 52.790  77.951  152.076 1.00 24.23 ? 262  LEU A N     1 
ATOM   2931  C  CA    . LEU I  3 262 ? 54.155  78.360  152.362 1.00 26.33 ? 262  LEU A CA    1 
ATOM   2932  C  C     . LEU I  3 262 ? 55.063  77.134  152.437 1.00 24.84 ? 262  LEU A C     1 
ATOM   2933  O  O     . LEU I  3 262 ? 56.160  77.128  151.883 1.00 26.91 ? 262  LEU A O     1 
ATOM   2934  C  CB    . LEU I  3 262 ? 54.215  79.098  153.696 1.00 28.38 ? 262  LEU A CB    1 
ATOM   2935  C  CG    . LEU I  3 262 ? 54.066  80.603  153.668 1.00 32.17 ? 262  LEU A CG    1 
ATOM   2936  C  CD1   . LEU I  3 262 ? 53.959  81.113  155.109 1.00 36.86 ? 262  LEU A CD1   1 
ATOM   2937  C  CD2   . LEU I  3 262 ? 55.265  81.215  152.964 1.00 33.82 ? 262  LEU A CD2   1 
ATOM   2938  N  N     . ASP I  3 263 ? 54.607  76.117  153.163 1.00 24.11 ? 263  ASP A N     1 
ATOM   2939  C  CA    . ASP I  3 263 ? 55.356  74.879  153.307 1.00 23.94 ? 263  ASP A CA    1 
ATOM   2940  C  C     . ASP I  3 263 ? 55.641  74.270  151.932 1.00 26.19 ? 263  ASP A C     1 
ATOM   2941  O  O     . ASP I  3 263 ? 56.757  73.815  151.668 1.00 24.31 ? 263  ASP A O     1 
ATOM   2942  C  CB    . ASP I  3 263 ? 54.573  73.867  154.152 1.00 26.92 ? 263  ASP A CB    1 
ATOM   2943  C  CG    . ASP I  3 263 ? 54.541  74.239  155.628 1.00 30.89 ? 263  ASP A CG    1 
ATOM   2944  O  OD1   . ASP I  3 263 ? 55.237  75.200  156.007 1.00 31.33 ? 263  ASP A OD1   1 
ATOM   2945  O  OD2   . ASP I  3 263 ? 53.836  73.563  156.405 1.00 33.76 ? 263  ASP A OD2   1 
ATOM   2946  N  N     . LEU I  3 264 ? 54.632  74.272  151.068 1.00 24.16 ? 264  LEU A N     1 
ATOM   2947  C  CA    . LEU I  3 264 ? 54.778  73.679  149.740 1.00 22.85 ? 264  LEU A CA    1 
ATOM   2948  C  C     . LEU I  3 264 ? 55.718  74.524  148.888 1.00 23.92 ? 264  LEU A C     1 
ATOM   2949  O  O     . LEU I  3 264 ? 56.575  73.982  148.165 1.00 21.78 ? 264  LEU A O     1 
ATOM   2950  C  CB    . LEU I  3 264 ? 53.400  73.512  149.091 1.00 23.37 ? 264  LEU A CB    1 
ATOM   2951  C  CG    . LEU I  3 264 ? 53.363  72.810  147.719 1.00 22.02 ? 264  LEU A CG    1 
ATOM   2952  C  CD1   . LEU I  3 264 ? 54.197  71.499  147.756 1.00 19.91 ? 264  LEU A CD1   1 
ATOM   2953  C  CD2   . LEU I  3 264 ? 51.920  72.520  147.347 1.00 21.25 ? 264  LEU A CD2   1 
ATOM   2954  N  N     . PHE I  3 265 ? 55.575  75.843  148.987 1.00 20.96 ? 265  PHE A N     1 
ATOM   2955  C  CA    . PHE I  3 265 ? 56.441  76.774  148.273 1.00 23.40 ? 265  PHE A CA    1 
ATOM   2956  C  C     . PHE I  3 265 ? 57.904  76.486  148.636 1.00 24.38 ? 265  PHE A C     1 
ATOM   2957  O  O     . PHE I  3 265 ? 58.751  76.376  147.752 1.00 20.92 ? 265  PHE A O     1 
ATOM   2958  C  CB    . PHE I  3 265 ? 56.106  78.225  148.666 1.00 22.31 ? 265  PHE A CB    1 
ATOM   2959  C  CG    . PHE I  3 265 ? 57.037  79.252  148.092 1.00 22.68 ? 265  PHE A CG    1 
ATOM   2960  C  CD1   . PHE I  3 265 ? 56.767  79.851  146.851 1.00 22.51 ? 265  PHE A CD1   1 
ATOM   2961  C  CD2   . PHE I  3 265 ? 58.161  79.672  148.806 1.00 19.97 ? 265  PHE A CD2   1 
ATOM   2962  C  CE1   . PHE I  3 265 ? 57.599  80.855  146.345 1.00 20.24 ? 265  PHE A CE1   1 
ATOM   2963  C  CE2   . PHE I  3 265 ? 58.993  80.668  148.316 1.00 22.51 ? 265  PHE A CE2   1 
ATOM   2964  C  CZ    . PHE I  3 265 ? 58.710  81.273  147.068 1.00 23.20 ? 265  PHE A CZ    1 
ATOM   2965  N  N     . TYR I  3 266 ? 58.223  76.384  149.932 1.00 20.85 ? 266  TYR A N     1 
ATOM   2966  C  CA    . TYR I  3 266 ? 59.615  76.111  150.297 1.00 22.37 ? 266  TYR A CA    1 
ATOM   2967  C  C     . TYR I  3 266 ? 60.087  74.713  149.946 1.00 21.16 ? 266  TYR A C     1 
ATOM   2968  O  O     . TYR I  3 266 ? 61.274  74.514  149.712 1.00 22.64 ? 266  TYR A O     1 
ATOM   2969  C  CB    . TYR I  3 266 ? 59.875  76.427  151.785 1.00 25.43 ? 266  TYR A CB    1 
ATOM   2970  C  CG    . TYR I  3 266 ? 59.883  77.918  152.028 1.00 26.98 ? 266  TYR A CG    1 
ATOM   2971  C  CD1   . TYR I  3 266 ? 58.895  78.523  152.802 1.00 28.98 ? 266  TYR A CD1   1 
ATOM   2972  C  CD2   . TYR I  3 266 ? 60.827  78.741  151.407 1.00 29.15 ? 266  TYR A CD2   1 
ATOM   2973  C  CE1   . TYR I  3 266 ? 58.839  79.908  152.947 1.00 31.29 ? 266  TYR A CE1   1 
ATOM   2974  C  CE2   . TYR I  3 266 ? 60.780  80.133  151.543 1.00 28.80 ? 266  TYR A CE2   1 
ATOM   2975  C  CZ    . TYR I  3 266 ? 59.779  80.707  152.315 1.00 32.80 ? 266  TYR A CZ    1 
ATOM   2976  O  OH    . TYR I  3 266 ? 59.698  82.076  152.452 1.00 34.25 ? 266  TYR A OH    1 
ATOM   2977  N  N     . ILE I  3 267 ? 59.183  73.742  149.893 1.00 21.04 ? 267  ILE A N     1 
ATOM   2978  C  CA    . ILE I  3 267 ? 59.590  72.393  149.494 1.00 21.28 ? 267  ILE A CA    1 
ATOM   2979  C  C     . ILE I  3 267 ? 60.096  72.493  148.057 1.00 23.29 ? 267  ILE A C     1 
ATOM   2980  O  O     . ILE I  3 267 ? 61.148  71.929  147.710 1.00 25.37 ? 267  ILE A O     1 
ATOM   2981  C  CB    . ILE I  3 267 ? 58.423  71.404  149.539 1.00 19.75 ? 267  ILE A CB    1 
ATOM   2982  C  CG1   . ILE I  3 267 ? 58.157  71.024  151.002 1.00 22.92 ? 267  ILE A CG1   1 
ATOM   2983  C  CG2   . ILE I  3 267 ? 58.756  70.140  148.729 1.00 23.77 ? 267  ILE A CG2   1 
ATOM   2984  C  CD1   . ILE I  3 267 ? 56.905  70.241  151.194 1.00 23.83 ? 267  ILE A CD1   1 
ATOM   2985  N  N     . MET I  3 268 ? 59.353  73.218  147.228 1.00 21.64 ? 268  MET A N     1 
ATOM   2986  C  CA    . MET I  3 268 ? 59.749  73.385  145.826 1.00 19.96 ? 268  MET A CA    1 
ATOM   2987  C  C     . MET I  3 268 ? 60.979  74.265  145.653 1.00 22.50 ? 268  MET A C     1 
ATOM   2988  O  O     . MET I  3 268 ? 61.870  73.930  144.868 1.00 22.98 ? 268  MET A O     1 
ATOM   2989  C  CB    . MET I  3 268 ? 58.586  73.950  144.996 1.00 21.17 ? 268  MET A CB    1 
ATOM   2990  C  CG    . MET I  3 268 ? 57.397  73.022  144.919 1.00 19.98 ? 268  MET A CG    1 
ATOM   2991  S  SD    . MET I  3 268 ? 56.112  73.617  143.812 1.00 19.66 ? 268  MET A SD    1 
ATOM   2992  C  CE    . MET I  3 268 ? 55.317  74.940  144.846 1.00 17.95 ? 268  MET A CE    1 
ATOM   2993  N  N     . VAL I  3 269 ? 61.068  75.376  146.378 1.00 21.96 ? 269  VAL A N     1 
ATOM   2994  C  CA    . VAL I  3 269 ? 62.225  76.251  146.226 1.00 21.54 ? 269  VAL A CA    1 
ATOM   2995  C  C     . VAL I  3 269 ? 63.486  75.656  146.856 1.00 25.63 ? 269  VAL A C     1 
ATOM   2996  O  O     . VAL I  3 269 ? 64.554  75.618  146.230 1.00 23.68 ? 269  VAL A O     1 
ATOM   2997  C  CB    . VAL I  3 269 ? 61.945  77.645  146.828 1.00 22.66 ? 269  VAL A CB    1 
ATOM   2998  C  CG1   . VAL I  3 269 ? 63.217  78.496  146.816 1.00 21.60 ? 269  VAL A CG1   1 
ATOM   2999  C  CG2   . VAL I  3 269 ? 60.822  78.325  146.035 1.00 20.45 ? 269  VAL A CG2   1 
ATOM   3000  N  N     . ASN I  3 270 ? 63.381  75.176  148.089 1.00 23.56 ? 270  ASN A N     1 
ATOM   3001  C  CA    . ASN I  3 270 ? 64.553  74.594  148.715 1.00 24.24 ? 270  ASN A CA    1 
ATOM   3002  C  C     . ASN I  3 270 ? 64.944  73.290  148.022 1.00 24.66 ? 270  ASN A C     1 
ATOM   3003  O  O     . ASN I  3 270 ? 66.119  72.898  148.043 1.00 26.63 ? 270  ASN A O     1 
ATOM   3004  C  CB    . ASN I  3 270 ? 64.302  74.342  150.202 1.00 25.73 ? 270  ASN A CB    1 
ATOM   3005  C  CG    . ASN I  3 270 ? 64.150  75.628  150.986 1.00 29.23 ? 270  ASN A CG    1 
ATOM   3006  O  OD1   . ASN I  3 270 ? 64.618  76.684  150.564 1.00 34.81 ? 270  ASN A OD1   1 
ATOM   3007  N  ND2   . ASN I  3 270 ? 63.508  75.541  152.149 1.00 32.27 ? 270  ASN A ND2   1 
ATOM   3008  N  N     . GLY I  3 271 ? 63.950  72.639  147.420 1.00 21.92 ? 271  GLY A N     1 
ATOM   3009  C  CA    . GLY I  3 271 ? 64.125  71.383  146.718 1.00 21.17 ? 271  GLY A CA    1 
ATOM   3010  C  C     . GLY I  3 271 ? 64.566  71.551  145.269 1.00 18.71 ? 271  GLY A C     1 
ATOM   3011  O  O     . GLY I  3 271 ? 64.532  70.594  144.504 1.00 21.04 ? 271  GLY A O     1 
ATOM   3012  N  N     . LYS I  3 272 ? 64.956  72.764  144.914 1.00 19.82 ? 272  LYS A N     1 
ATOM   3013  C  CA    . LYS I  3 272 ? 65.460  73.049  143.567 1.00 21.92 ? 272  LYS A CA    1 
ATOM   3014  C  C     . LYS I  3 272 ? 64.504  72.673  142.447 1.00 20.07 ? 272  LYS A C     1 
ATOM   3015  O  O     . LYS I  3 272 ? 64.941  72.181  141.397 1.00 19.90 ? 272  LYS A O     1 
ATOM   3016  C  CB    . LYS I  3 272 ? 66.795  72.315  143.349 1.00 25.10 ? 272  LYS A CB    1 
ATOM   3017  C  CG    . LYS I  3 272 ? 67.831  72.576  144.443 1.00 29.36 ? 272  LYS A CG    1 
ATOM   3018  C  CD    . LYS I  3 272 ? 68.085  74.051  144.646 1.00 39.46 ? 272  LYS A CD    1 
ATOM   3019  C  CE    . LYS I  3 272 ? 69.031  74.306  145.820 1.00 47.12 ? 272  LYS A CE    1 
ATOM   3020  N  NZ    . LYS I  3 272 ? 69.205  75.765  146.105 1.00 49.41 ? 272  LYS A NZ    1 
ATOM   3021  N  N     . ARG I  3 273 ? 63.203  72.887  142.659 1.00 19.28 ? 273  ARG A N     1 
ATOM   3022  C  CA    . ARG I  3 273 ? 62.213  72.582  141.614 1.00 18.61 ? 273  ARG A CA    1 
ATOM   3023  C  C     . ARG I  3 273 ? 61.542  73.847  141.122 1.00 16.92 ? 273  ARG A C     1 
ATOM   3024  O  O     . ARG I  3 273 ? 60.886  73.841  140.084 1.00 17.77 ? 273  ARG A O     1 
ATOM   3025  C  CB    . ARG I  3 273 ? 61.098  71.638  142.090 1.00 19.73 ? 273  ARG A CB    1 
ATOM   3026  C  CG    . ARG I  3 273 ? 61.558  70.369  142.806 1.00 18.58 ? 273  ARG A CG    1 
ATOM   3027  C  CD    . ARG I  3 273 ? 62.631  69.618  142.010 1.00 15.26 ? 273  ARG A CD    1 
ATOM   3028  N  NE    . ARG I  3 273 ? 62.142  69.090  140.732 1.00 15.88 ? 273  ARG A NE    1 
ATOM   3029  C  CZ    . ARG I  3 273 ? 62.722  69.335  139.555 1.00 16.01 ? 273  ARG A CZ    1 
ATOM   3030  N  NH1   . ARG I  3 273 ? 63.797  70.114  139.492 1.00 18.31 ? 273  ARG A NH1   1 
ATOM   3031  N  NH2   . ARG I  3 273 ? 62.255  68.757  138.449 1.00 18.33 ? 273  ARG A NH2   1 
ATOM   3032  N  N     . LEU I  3 274 ? 61.708  74.930  141.875 1.00 16.42 ? 274  LEU A N     1 
ATOM   3033  C  CA    . LEU I  3 274 ? 61.089  76.211  141.540 1.00 16.33 ? 274  LEU A CA    1 
ATOM   3034  C  C     . LEU I  3 274 ? 62.019  77.401  141.797 1.00 16.64 ? 274  LEU A C     1 
ATOM   3035  O  O     . LEU I  3 274 ? 62.639  77.506  142.870 1.00 18.02 ? 274  LEU A O     1 
ATOM   3036  C  CB    . LEU I  3 274 ? 59.784  76.383  142.360 1.00 15.85 ? 274  LEU A CB    1 
ATOM   3037  C  CG    . LEU I  3 274 ? 58.974  77.636  142.051 1.00 18.17 ? 274  LEU A CG    1 
ATOM   3038  C  CD1   . LEU I  3 274 ? 58.493  77.608  140.576 1.00 16.18 ? 274  LEU A CD1   1 
ATOM   3039  C  CD2   . LEU I  3 274 ? 57.782  77.718  143.021 1.00 19.75 ? 274  LEU A CD2   1 
ATOM   3040  N  N     . LYS I  3 275 ? 62.132  78.293  140.808 1.00 15.30 ? 275  LYS A N     1 
ATOM   3041  C  CA    . LYS I  3 275 ? 62.967  79.480  140.909 1.00 17.82 ? 275  LYS A CA    1 
ATOM   3042  C  C     . LYS I  3 275 ? 62.211  80.683  140.342 1.00 14.84 ? 275  LYS A C     1 
ATOM   3043  O  O     . LYS I  3 275 ? 61.040  80.566  139.985 1.00 18.90 ? 275  LYS A O     1 
ATOM   3044  C  CB    . LYS I  3 275 ? 64.281  79.278  140.132 1.00 17.50 ? 275  LYS A CB    1 
ATOM   3045  C  CG    . LYS I  3 275 ? 65.149  78.123  140.654 1.00 17.79 ? 275  LYS A CG    1 
ATOM   3046  C  CD    . LYS I  3 275 ? 66.422  77.967  139.808 1.00 18.52 ? 275  LYS A CD    1 
ATOM   3047  C  CE    . LYS I  3 275 ? 67.267  76.761  140.250 1.00 18.73 ? 275  LYS A CE    1 
ATOM   3048  N  NZ    . LYS I  3 275 ? 68.645  76.841  139.609 1.00 20.22 ? 275  LYS A NZ    1 
ATOM   3049  N  N     . ASP I  3 276 ? 62.882  81.830  140.262 1.00 14.27 ? 276  ASP A N     1 
ATOM   3050  C  CA    . ASP I  3 276 ? 62.258  83.040  139.738 1.00 17.42 ? 276  ASP A CA    1 
ATOM   3051  C  C     . ASP I  3 276 ? 62.589  83.176  138.247 1.00 17.82 ? 276  ASP A C     1 
ATOM   3052  O  O     . ASP I  3 276 ? 63.600  82.634  137.794 1.00 18.02 ? 276  ASP A O     1 
ATOM   3053  C  CB    . ASP I  3 276 ? 62.821  84.280  140.435 1.00 19.99 ? 276  ASP A CB    1 
ATOM   3054  C  CG    . ASP I  3 276 ? 62.165  85.558  139.952 1.00 19.47 ? 276  ASP A CG    1 
ATOM   3055  O  OD1   . ASP I  3 276 ? 60.939  85.700  140.139 1.00 22.10 ? 276  ASP A OD1   1 
ATOM   3056  O  OD2   . ASP I  3 276 ? 62.860  86.417  139.391 1.00 19.77 ? 276  ASP A OD2   1 
ATOM   3057  N  N     . ILE I  3 277 ? 61.763  83.916  137.509 1.00 17.70 ? 277  ILE A N     1 
ATOM   3058  C  CA    . ILE I  3 277 ? 62.015  84.139  136.071 1.00 18.00 ? 277  ILE A CA    1 
ATOM   3059  C  C     . ILE I  3 277 ? 63.452  84.698  135.873 1.00 20.94 ? 277  ILE A C     1 
ATOM   3060  O  O     . ILE I  3 277 ? 64.121  84.368  134.889 1.00 17.75 ? 277  ILE A O     1 
ATOM   3061  C  CB    . ILE I  3 277 ? 60.950  85.137  135.468 1.00 22.32 ? 277  ILE A CB    1 
ATOM   3062  C  CG1   . ILE I  3 277 ? 61.202  85.400  133.980 1.00 22.32 ? 277  ILE A CG1   1 
ATOM   3063  C  CG2   . ILE I  3 277 ? 60.971  86.459  136.220 1.00 21.24 ? 277  ILE A CG2   1 
ATOM   3064  C  CD1   . ILE I  3 277 ? 61.018  84.214  133.124 1.00 22.79 ? 277  ILE A CD1   1 
ATOM   3065  N  N     . SER I  3 278 ? 63.944  85.507  136.822 1.00 16.73 ? 278  SER A N     1 
ATOM   3066  C  CA    . SER I  3 278 ? 65.287  86.091  136.697 1.00 18.30 ? 278  SER A CA    1 
ATOM   3067  C  C     . SER I  3 278 ? 66.433  85.076  136.806 1.00 19.25 ? 278  SER A C     1 
ATOM   3068  O  O     . SER I  3 278 ? 67.576  85.378  136.463 1.00 20.54 ? 278  SER A O     1 
ATOM   3069  C  CB    . SER I  3 278 ? 65.502  87.228  137.747 1.00 18.51 ? 278  SER A CB    1 
ATOM   3070  O  OG    . SER I  3 278 ? 65.624  86.723  139.059 1.00 19.37 ? 278  SER A OG    1 
ATOM   3071  N  N     . ASP I  3 279 ? 66.138  83.883  137.294 1.00 16.99 ? 279  ASP A N     1 
ATOM   3072  C  CA    . ASP I  3 279 ? 67.157  82.837  137.413 1.00 18.09 ? 279  ASP A CA    1 
ATOM   3073  C  C     . ASP I  3 279 ? 67.335  82.114  136.076 1.00 17.93 ? 279  ASP A C     1 
ATOM   3074  O  O     . ASP I  3 279 ? 68.376  81.474  135.824 1.00 17.71 ? 279  ASP A O     1 
ATOM   3075  C  CB    . ASP I  3 279 ? 66.710  81.814  138.455 1.00 18.71 ? 279  ASP A CB    1 
ATOM   3076  C  CG    . ASP I  3 279 ? 66.731  82.379  139.850 1.00 22.11 ? 279  ASP A CG    1 
ATOM   3077  O  OD1   . ASP I  3 279 ? 67.814  82.836  140.239 1.00 19.13 ? 279  ASP A OD1   1 
ATOM   3078  O  OD2   . ASP I  3 279 ? 65.681  82.369  140.536 1.00 19.79 ? 279  ASP A OD2   1 
ATOM   3079  N  N     . LEU I  3 280 ? 66.337  82.234  135.211 1.00 16.57 ? 280  LEU A N     1 
ATOM   3080  C  CA    . LEU I  3 280 ? 66.377  81.490  133.953 1.00 17.55 ? 280  LEU A CA    1 
ATOM   3081  C  C     . LEU I  3 280 ? 67.529  81.800  133.000 1.00 17.56 ? 280  LEU A C     1 
ATOM   3082  O  O     . LEU I  3 280 ? 68.210  80.868  132.530 1.00 17.72 ? 280  LEU A O     1 
ATOM   3083  C  CB    . LEU I  3 280 ? 65.033  81.599  133.219 1.00 18.64 ? 280  LEU A CB    1 
ATOM   3084  C  CG    . LEU I  3 280 ? 64.960  80.782  131.917 1.00 18.27 ? 280  LEU A CG    1 
ATOM   3085  C  CD1   . LEU I  3 280 ? 65.330  79.309  132.182 1.00 17.78 ? 280  LEU A CD1   1 
ATOM   3086  C  CD2   . LEU I  3 280 ? 63.559  80.891  131.330 1.00 20.24 ? 280  LEU A CD2   1 
ATOM   3087  N  N     . PRO I  3 281 ? 67.783  83.085  132.692 1.00 18.43 ? 281  PRO A N     1 
ATOM   3088  C  CA    . PRO I  3 281 ? 68.897  83.378  131.769 1.00 18.83 ? 281  PRO A CA    1 
ATOM   3089  C  C     . PRO I  3 281 ? 70.222  82.785  132.238 1.00 19.00 ? 281  PRO A C     1 
ATOM   3090  O  O     . PRO I  3 281 ? 70.939  82.153  131.457 1.00 19.55 ? 281  PRO A O     1 
ATOM   3091  C  CB    . PRO I  3 281 ? 68.932  84.903  131.736 1.00 20.33 ? 281  PRO A CB    1 
ATOM   3092  C  CG    . PRO I  3 281 ? 67.502  85.285  132.005 1.00 18.39 ? 281  PRO A CG    1 
ATOM   3093  C  CD    . PRO I  3 281 ? 67.106  84.326  133.108 1.00 16.62 ? 281  PRO A CD    1 
ATOM   3094  N  N     . LEU I  3 282 ? 70.545  82.943  133.522 1.00 18.52 ? 282  LEU A N     1 
ATOM   3095  C  CA    . LEU I  3 282 ? 71.788  82.374  134.047 1.00 19.42 ? 282  LEU A CA    1 
ATOM   3096  C  C     . LEU I  3 282 ? 71.760  80.839  134.053 1.00 19.52 ? 282  LEU A C     1 
ATOM   3097  O  O     . LEU I  3 282 ? 72.789  80.197  133.818 1.00 17.77 ? 282  LEU A O     1 
ATOM   3098  C  CB    . LEU I  3 282 ? 72.072  82.897  135.468 1.00 22.39 ? 282  LEU A CB    1 
ATOM   3099  C  CG    . LEU I  3 282 ? 72.950  84.147  135.542 1.00 23.59 ? 282  LEU A CG    1 
ATOM   3100  C  CD1   . LEU I  3 282 ? 72.885  84.724  136.962 1.00 24.40 ? 282  LEU A CD1   1 
ATOM   3101  C  CD2   . LEU I  3 282 ? 74.405  83.806  135.158 1.00 24.09 ? 282  LEU A CD2   1 
ATOM   3102  N  N     . ASP I  3 283 ? 70.599  80.232  134.324 1.00 17.24 ? 283  ASP A N     1 
ATOM   3103  C  CA    . ASP I  3 283 ? 70.533  78.772  134.307 1.00 13.52 ? 283  ASP A CA    1 
ATOM   3104  C  C     . ASP I  3 283 ? 70.729  78.243  132.868 1.00 16.68 ? 283  ASP A C     1 
ATOM   3105  O  O     . ASP I  3 283 ? 71.182  77.126  132.684 1.00 18.62 ? 283  ASP A O     1 
ATOM   3106  C  CB    . ASP I  3 283 ? 69.213  78.275  134.900 1.00 17.11 ? 283  ASP A CB    1 
ATOM   3107  C  CG    . ASP I  3 283 ? 69.259  78.213  136.425 1.00 20.67 ? 283  ASP A CG    1 
ATOM   3108  O  OD1   . ASP I  3 283 ? 70.343  78.462  136.994 1.00 18.05 ? 283  ASP A OD1   1 
ATOM   3109  O  OD2   . ASP I  3 283 ? 68.223  77.896  137.033 1.00 18.16 ? 283  ASP A OD2   1 
ATOM   3110  N  N     . LEU I  3 284 ? 70.394  79.049  131.863 1.00 17.45 ? 284  LEU A N     1 
ATOM   3111  C  CA    . LEU I  3 284 ? 70.615  78.643  130.474 1.00 14.89 ? 284  LEU A CA    1 
ATOM   3112  C  C     . LEU I  3 284 ? 72.105  78.782  130.096 1.00 18.35 ? 284  LEU A C     1 
ATOM   3113  O  O     . LEU I  3 284 ? 72.511  78.398  128.996 1.00 17.55 ? 284  LEU A O     1 
ATOM   3114  C  CB    . LEU I  3 284 ? 69.781  79.516  129.537 1.00 17.57 ? 284  LEU A CB    1 
ATOM   3115  C  CG    . LEU I  3 284 ? 68.258  79.305  129.580 1.00 19.77 ? 284  LEU A CG    1 
ATOM   3116  C  CD1   . LEU I  3 284 ? 67.603  80.313  128.649 1.00 19.61 ? 284  LEU A CD1   1 
ATOM   3117  C  CD2   . LEU I  3 284 ? 67.880  77.884  129.175 1.00 18.79 ? 284  LEU A CD2   1 
ATOM   3118  N  N     . ALA I  3 285 ? 72.923  79.326  130.989 1.00 17.90 ? 285  ALA A N     1 
ATOM   3119  C  CA    . ALA I  3 285 ? 74.349  79.493  130.694 1.00 17.62 ? 285  ALA A CA    1 
ATOM   3120  C  C     . ALA I  3 285 ? 75.249  78.403  131.300 1.00 16.33 ? 285  ALA A C     1 
ATOM   3121  O  O     . ALA I  3 285 ? 76.475  78.487  131.175 1.00 18.14 ? 285  ALA A O     1 
ATOM   3122  C  CB    . ALA I  3 285 ? 74.818  80.871  131.193 1.00 20.11 ? 285  ALA A CB    1 
ATOM   3123  N  N     . VAL I  3 286 ? 74.679  77.378  131.939 1.00 17.97 ? 286  VAL A N     1 
ATOM   3124  C  CA    . VAL I  3 286 ? 75.529  76.356  132.569 1.00 21.83 ? 286  VAL A CA    1 
ATOM   3125  C  C     . VAL I  3 286 ? 76.384  75.562  131.561 1.00 22.76 ? 286  VAL A C     1 
ATOM   3126  O  O     . VAL I  3 286 ? 77.531  75.141  131.919 1.00 18.55 ? 286  VAL A O     1 
ATOM   3127  C  CB    . VAL I  3 286 ? 74.702  75.343  133.399 1.00 22.33 ? 286  VAL A CB    1 
ATOM   3128  C  CG1   . VAL I  3 286 ? 73.958  76.057  134.539 1.00 20.76 ? 286  VAL A CG1   1 
ATOM   3129  C  CG2   . VAL I  3 286 ? 73.750  74.611  132.493 1.00 25.35 ? 286  VAL A CG2   1 
ATOM   3130  O  OXT   . VAL I  3 286 ? 75.875  75.352  130.431 1.00 21.41 ? 286  VAL A OXT   1 
ATOM   3131  N  N     . MET J  3 1   ? 19.190  35.149  118.718 1.00 56.27 ? 1    MET B N     1 
ATOM   3132  C  CA    . MET J  3 1   ? 19.627  35.875  119.946 1.00 54.35 ? 1    MET B CA    1 
ATOM   3133  C  C     . MET J  3 1   ? 20.948  36.600  119.698 1.00 51.65 ? 1    MET B C     1 
ATOM   3134  O  O     . MET J  3 1   ? 21.872  36.052  119.092 1.00 52.67 ? 1    MET B O     1 
ATOM   3135  C  CB    . MET J  3 1   ? 19.802  34.887  121.107 1.00 56.41 ? 1    MET B CB    1 
ATOM   3136  C  CG    . MET J  3 1   ? 20.110  35.535  122.455 1.00 57.65 ? 1    MET B CG    1 
ATOM   3137  S  SD    . MET J  3 1   ? 20.548  34.308  123.720 1.00 60.04 ? 1    MET B SD    1 
ATOM   3138  C  CE    . MET J  3 1   ? 21.945  35.125  124.551 1.00 54.11 ? 1    MET B CE    1 
ATOM   3139  N  N     . GLN J  3 2   ? 21.033  37.845  120.147 1.00 48.84 ? 2    GLN B N     1 
ATOM   3140  C  CA    . GLN J  3 2   ? 22.269  38.591  119.991 1.00 44.86 ? 2    GLN B CA    1 
ATOM   3141  C  C     . GLN J  3 2   ? 23.161  38.211  121.169 1.00 38.13 ? 2    GLN B C     1 
ATOM   3142  O  O     . GLN J  3 2   ? 22.668  37.970  122.272 1.00 34.62 ? 2    GLN B O     1 
ATOM   3143  C  CB    . GLN J  3 2   ? 21.993  40.098  119.982 1.00 47.64 ? 2    GLN B CB    1 
ATOM   3144  C  CG    . GLN J  3 2   ? 21.278  40.565  118.727 1.00 55.08 ? 2    GLN B CG    1 
ATOM   3145  C  CD    . GLN J  3 2   ? 21.956  40.067  117.456 1.00 58.09 ? 2    GLN B CD    1 
ATOM   3146  O  OE1   . GLN J  3 2   ? 23.138  40.332  117.224 1.00 60.04 ? 2    GLN B OE1   1 
ATOM   3147  N  NE2   . GLN J  3 2   ? 21.209  39.340  116.627 1.00 60.04 ? 2    GLN B NE2   1 
ATOM   3148  N  N     . PRO J  3 3   ? 24.481  38.125  120.937 1.00 34.42 ? 3    PRO B N     1 
ATOM   3149  C  CA    . PRO J  3 3   ? 25.459  37.771  121.974 1.00 33.44 ? 3    PRO B CA    1 
ATOM   3150  C  C     . PRO J  3 3   ? 25.295  38.672  123.198 1.00 34.11 ? 3    PRO B C     1 
ATOM   3151  O  O     . PRO J  3 3   ? 24.878  39.825  123.078 1.00 32.75 ? 3    PRO B O     1 
ATOM   3152  C  CB    . PRO J  3 3   ? 26.796  37.996  121.276 1.00 35.76 ? 3    PRO B CB    1 
ATOM   3153  C  CG    . PRO J  3 3   ? 26.500  37.689  119.849 1.00 36.52 ? 3    PRO B CG    1 
ATOM   3154  C  CD    . PRO J  3 3   ? 25.146  38.343  119.639 1.00 32.40 ? 3    PRO B CD    1 
ATOM   3155  N  N     . LEU J  3 4   ? 25.634  38.160  124.376 1.00 32.34 ? 4    LEU B N     1 
ATOM   3156  C  CA    . LEU J  3 4   ? 25.495  38.961  125.586 1.00 31.37 ? 4    LEU B CA    1 
ATOM   3157  C  C     . LEU J  3 4   ? 26.396  40.203  125.618 1.00 29.61 ? 4    LEU B C     1 
ATOM   3158  O  O     . LEU J  3 4   ? 26.039  41.213  126.240 1.00 27.30 ? 4    LEU B O     1 
ATOM   3159  C  CB    . LEU J  3 4   ? 25.737  38.102  126.827 1.00 32.88 ? 4    LEU B CB    1 
ATOM   3160  C  CG    . LEU J  3 4   ? 24.664  37.044  127.103 1.00 33.85 ? 4    LEU B CG    1 
ATOM   3161  C  CD1   . LEU J  3 4   ? 24.899  36.441  128.483 1.00 34.46 ? 4    LEU B CD1   1 
ATOM   3162  C  CD2   . LEU J  3 4   ? 23.271  37.681  127.041 1.00 35.25 ? 4    LEU B CD2   1 
ATOM   3163  N  N     . PHE J  3 5   ? 27.544  40.136  124.957 1.00 27.52 ? 5    PHE B N     1 
ATOM   3164  C  CA    . PHE J  3 5   ? 28.432  41.295  124.944 1.00 28.80 ? 5    PHE B CA    1 
ATOM   3165  C  C     . PHE J  3 5   ? 27.855  42.360  124.032 1.00 30.65 ? 5    PHE B C     1 
ATOM   3166  O  O     . PHE J  3 5   ? 28.029  43.561  124.278 1.00 28.27 ? 5    PHE B O     1 
ATOM   3167  C  CB    . PHE J  3 5   ? 29.847  40.917  124.507 1.00 30.37 ? 5    PHE B CB    1 
ATOM   3168  C  CG    . PHE J  3 5   ? 30.682  40.309  125.614 1.00 27.37 ? 5    PHE B CG    1 
ATOM   3169  C  CD1   . PHE J  3 5   ? 31.960  39.844  125.358 1.00 30.69 ? 5    PHE B CD1   1 
ATOM   3170  C  CD2   . PHE J  3 5   ? 30.191  40.221  126.915 1.00 29.37 ? 5    PHE B CD2   1 
ATOM   3171  C  CE1   . PHE J  3 5   ? 32.753  39.296  126.389 1.00 32.61 ? 5    PHE B CE1   1 
ATOM   3172  C  CE2   . PHE J  3 5   ? 30.975  39.674  127.952 1.00 31.78 ? 5    PHE B CE2   1 
ATOM   3173  C  CZ    . PHE J  3 5   ? 32.257  39.215  127.681 1.00 26.23 ? 5    PHE B CZ    1 
ATOM   3174  N  N     . THR J  3 6   ? 27.167  41.929  122.977 1.00 30.03 ? 6    THR B N     1 
ATOM   3175  C  CA    . THR J  3 6   ? 26.544  42.903  122.076 1.00 29.97 ? 6    THR B CA    1 
ATOM   3176  C  C     . THR J  3 6   ? 25.419  43.577  122.867 1.00 29.58 ? 6    THR B C     1 
ATOM   3177  O  O     . THR J  3 6   ? 25.188  44.780  122.739 1.00 27.62 ? 6    THR B O     1 
ATOM   3178  C  CB    . THR J  3 6   ? 25.953  42.242  120.825 1.00 30.88 ? 6    THR B CB    1 
ATOM   3179  O  OG1   . THR J  3 6   ? 26.990  41.582  120.096 1.00 31.73 ? 6    THR B OG1   1 
ATOM   3180  C  CG2   . THR J  3 6   ? 25.312  43.307  119.923 1.00 32.59 ? 6    THR B CG2   1 
ATOM   3181  N  N     . GLN J  3 7   ? 24.735  42.797  123.703 1.00 28.51 ? 7    GLN B N     1 
ATOM   3182  C  CA    . GLN J  3 7   ? 23.671  43.330  124.538 1.00 30.27 ? 7    GLN B CA    1 
ATOM   3183  C  C     . GLN J  3 7   ? 24.236  44.279  125.595 1.00 33.19 ? 7    GLN B C     1 
ATOM   3184  O  O     . GLN J  3 7   ? 23.617  45.301  125.930 1.00 32.51 ? 7    GLN B O     1 
ATOM   3185  C  CB    . GLN J  3 7   ? 22.905  42.194  125.219 1.00 32.22 ? 7    GLN B CB    1 
ATOM   3186  C  CG    . GLN J  3 7   ? 22.003  41.417  124.272 1.00 33.26 ? 7    GLN B CG    1 
ATOM   3187  C  CD    . GLN J  3 7   ? 21.257  40.297  124.969 1.00 35.11 ? 7    GLN B CD    1 
ATOM   3188  O  OE1   . GLN J  3 7   ? 20.689  40.488  126.052 1.00 36.91 ? 7    GLN B OE1   1 
ATOM   3189  N  NE2   . GLN J  3 7   ? 21.248  39.117  124.351 1.00 35.38 ? 7    GLN B NE2   1 
ATOM   3190  N  N     . GLU J  3 8   ? 25.405  43.939  126.136 1.00 29.76 ? 8    GLU B N     1 
ATOM   3191  C  CA    . GLU J  3 8   ? 26.039  44.796  127.135 1.00 31.04 ? 8    GLU B CA    1 
ATOM   3192  C  C     . GLU J  3 8   ? 26.440  46.136  126.516 1.00 24.59 ? 8    GLU B C     1 
ATOM   3193  O  O     . GLU J  3 8   ? 26.296  47.190  127.142 1.00 27.40 ? 8    GLU B O     1 
ATOM   3194  C  CB    . GLU J  3 8   ? 27.285  44.116  127.711 1.00 31.35 ? 8    GLU B CB    1 
ATOM   3195  C  CG    . GLU J  3 8   ? 27.018  42.945  128.645 1.00 39.05 ? 8    GLU B CG    1 
ATOM   3196  C  CD    . GLU J  3 8   ? 26.322  43.355  129.930 1.00 43.93 ? 8    GLU B CD    1 
ATOM   3197  O  OE1   . GLU J  3 8   ? 26.555  44.486  130.413 1.00 48.86 ? 8    GLU B OE1   1 
ATOM   3198  O  OE2   . GLU J  3 8   ? 25.550  42.537  130.469 1.00 50.36 ? 8    GLU B OE2   1 
ATOM   3199  N  N     . ARG J  3 9   ? 26.949  46.082  125.294 1.00 25.37 ? 9    ARG B N     1 
ATOM   3200  C  CA    . ARG J  3 9   ? 27.371  47.279  124.577 1.00 25.97 ? 9    ARG B CA    1 
ATOM   3201  C  C     . ARG J  3 9   ? 26.170  48.194  124.371 1.00 29.21 ? 9    ARG B C     1 
ATOM   3202  O  O     . ARG J  3 9   ? 26.283  49.409  124.503 1.00 27.51 ? 9    ARG B O     1 
ATOM   3203  C  CB    . ARG J  3 9   ? 27.965  46.898  123.233 1.00 24.54 ? 9    ARG B CB    1 
ATOM   3204  C  CG    . ARG J  3 9   ? 28.684  48.039  122.490 1.00 25.30 ? 9    ARG B CG    1 
ATOM   3205  C  CD    . ARG J  3 9   ? 29.218  47.540  121.139 1.00 21.19 ? 9    ARG B CD    1 
ATOM   3206  N  NE    . ARG J  3 9   ? 30.061  48.514  120.452 1.00 24.39 ? 9    ARG B NE    1 
ATOM   3207  C  CZ    . ARG J  3 9   ? 29.655  49.315  119.467 1.00 29.79 ? 9    ARG B CZ    1 
ATOM   3208  N  NH1   . ARG J  3 9   ? 28.396  49.264  119.031 1.00 28.23 ? 9    ARG B NH1   1 
ATOM   3209  N  NH2   . ARG J  3 9   ? 30.506  50.171  118.917 1.00 25.08 ? 9    ARG B NH2   1 
ATOM   3210  N  N     . ARG J  3 10  ? 25.015  47.606  124.059 1.00 28.88 ? 10   ARG B N     1 
ATOM   3211  C  CA    . ARG J  3 10  ? 23.801  48.409  123.863 1.00 29.27 ? 10   ARG B CA    1 
ATOM   3212  C  C     . ARG J  3 10  ? 23.309  49.068  125.160 1.00 28.32 ? 10   ARG B C     1 
ATOM   3213  O  O     . ARG J  3 10  ? 22.871  50.232  125.141 1.00 28.54 ? 10   ARG B O     1 
ATOM   3214  C  CB    . ARG J  3 10  ? 22.704  47.545  123.224 1.00 31.77 ? 10   ARG B CB    1 
ATOM   3215  C  CG    . ARG J  3 10  ? 23.097  47.077  121.816 1.00 39.00 ? 10   ARG B CG    1 
ATOM   3216  C  CD    . ARG J  3 10  ? 22.081  46.151  121.158 1.00 44.58 ? 10   ARG B CD    1 
ATOM   3217  N  NE    . ARG J  3 10  ? 22.487  45.805  119.796 1.00 49.87 ? 10   ARG B NE    1 
ATOM   3218  C  CZ    . ARG J  3 10  ? 21.818  44.971  119.005 1.00 55.33 ? 10   ARG B CZ    1 
ATOM   3219  N  NH1   . ARG J  3 10  ? 20.707  44.397  119.444 1.00 57.74 ? 10   ARG B NH1   1 
ATOM   3220  N  NH2   . ARG J  3 10  ? 22.254  44.709  117.776 1.00 55.87 ? 10   ARG B NH2   1 
ATOM   3221  N  N     . ILE J  3 11  ? 23.375  48.341  126.278 1.00 26.12 ? 11   ILE B N     1 
ATOM   3222  C  CA    . ILE J  3 11  ? 22.987  48.874  127.578 1.00 27.08 ? 11   ILE B CA    1 
ATOM   3223  C  C     . ILE J  3 11  ? 23.908  50.064  127.912 1.00 27.09 ? 11   ILE B C     1 
ATOM   3224  O  O     . ILE J  3 11  ? 23.454  51.081  128.429 1.00 26.74 ? 11   ILE B O     1 
ATOM   3225  C  CB    . ILE J  3 11  ? 23.117  47.800  128.684 1.00 27.65 ? 11   ILE B CB    1 
ATOM   3226  C  CG1   . ILE J  3 11  ? 22.032  46.738  128.506 1.00 30.61 ? 11   ILE B CG1   1 
ATOM   3227  C  CG2   . ILE J  3 11  ? 23.025  48.437  130.057 1.00 28.82 ? 11   ILE B CG2   1 
ATOM   3228  C  CD1   . ILE J  3 11  ? 22.095  45.631  129.555 1.00 30.42 ? 11   ILE B CD1   1 
ATOM   3229  N  N     . PHE J  3 12  ? 25.199  49.908  127.613 1.00 27.54 ? 12   PHE B N     1 
ATOM   3230  C  CA    . PHE J  3 12  ? 26.220  50.949  127.846 1.00 26.41 ? 12   PHE B CA    1 
ATOM   3231  C  C     . PHE J  3 12  ? 25.774  52.234  127.133 1.00 25.58 ? 12   PHE B C     1 
ATOM   3232  O  O     . PHE J  3 12  ? 25.657  53.314  127.732 1.00 24.42 ? 12   PHE B O     1 
ATOM   3233  C  CB    . PHE J  3 12  ? 27.568  50.425  127.296 1.00 23.71 ? 12   PHE B CB    1 
ATOM   3234  C  CG    . PHE J  3 12  ? 28.668  51.460  127.194 1.00 25.70 ? 12   PHE B CG    1 
ATOM   3235  C  CD1   . PHE J  3 12  ? 29.289  51.971  128.337 1.00 24.68 ? 12   PHE B CD1   1 
ATOM   3236  C  CD2   . PHE J  3 12  ? 29.112  51.889  125.946 1.00 24.47 ? 12   PHE B CD2   1 
ATOM   3237  C  CE1   . PHE J  3 12  ? 30.343  52.909  128.232 1.00 24.60 ? 12   PHE B CE1   1 
ATOM   3238  C  CE2   . PHE J  3 12  ? 30.159  52.817  125.829 1.00 25.39 ? 12   PHE B CE2   1 
ATOM   3239  C  CZ    . PHE J  3 12  ? 30.771  53.323  126.977 1.00 24.05 ? 12   PHE B CZ    1 
ATOM   3240  N  N     . HIS J  3 13  ? 25.521  52.100  125.848 1.00 24.08 ? 13   HIS B N     1 
ATOM   3241  C  CA    . HIS J  3 13  ? 25.054  53.222  125.035 1.00 28.57 ? 13   HIS B CA    1 
ATOM   3242  C  C     . HIS J  3 13  ? 23.725  53.795  125.559 1.00 27.96 ? 13   HIS B C     1 
ATOM   3243  O  O     . HIS J  3 13  ? 23.563  55.014  125.640 1.00 28.33 ? 13   HIS B O     1 
ATOM   3244  C  CB    . HIS J  3 13  ? 24.900  52.766  123.590 1.00 26.94 ? 13   HIS B CB    1 
ATOM   3245  C  CG    . HIS J  3 13  ? 26.195  52.622  122.858 1.00 27.67 ? 13   HIS B CG    1 
ATOM   3246  N  ND1   . HIS J  3 13  ? 26.325  51.856  121.722 1.00 27.50 ? 13   HIS B ND1   1 
ATOM   3247  C  CD2   . HIS J  3 13  ? 27.416  53.167  123.085 1.00 25.70 ? 13   HIS B CD2   1 
ATOM   3248  C  CE1   . HIS J  3 13  ? 27.568  51.932  121.280 1.00 30.47 ? 13   HIS B CE1   1 
ATOM   3249  N  NE2   . HIS J  3 13  ? 28.249  52.724  122.091 1.00 28.05 ? 13   HIS B NE2   1 
ATOM   3250  N  N     . LYS J  3 14  ? 22.775  52.929  125.920 1.00 28.36 ? 14   LYS B N     1 
ATOM   3251  C  CA    . LYS J  3 14  ? 21.492  53.407  126.451 1.00 28.39 ? 14   LYS B CA    1 
ATOM   3252  C  C     . LYS J  3 14  ? 21.642  54.240  127.712 1.00 29.62 ? 14   LYS B C     1 
ATOM   3253  O  O     . LYS J  3 14  ? 20.862  55.166  127.962 1.00 27.50 ? 14   LYS B O     1 
ATOM   3254  C  CB    . LYS J  3 14  ? 20.543  52.234  126.763 1.00 32.50 ? 14   LYS B CB    1 
ATOM   3255  C  CG    . LYS J  3 14  ? 19.858  51.648  125.546 1.00 37.35 ? 14   LYS B CG    1 
ATOM   3256  C  CD    . LYS J  3 14  ? 18.980  50.437  125.923 1.00 39.78 ? 14   LYS B CD    1 
ATOM   3257  C  CE    . LYS J  3 14  ? 17.900  50.767  126.967 1.00 41.31 ? 14   LYS B CE    1 
ATOM   3258  N  NZ    . LYS J  3 14  ? 16.830  51.713  126.493 1.00 35.02 ? 14   LYS B NZ    1 
ATOM   3259  N  N     . LYS J  3 15  ? 22.620  53.912  128.543 1.00 24.62 ? 15   LYS B N     1 
ATOM   3260  C  CA    . LYS J  3 15  ? 22.792  54.690  129.755 1.00 25.51 ? 15   LYS B CA    1 
ATOM   3261  C  C     . LYS J  3 15  ? 23.281  56.087  129.403 1.00 25.09 ? 15   LYS B C     1 
ATOM   3262  O  O     . LYS J  3 15  ? 22.898  57.050  130.058 1.00 25.98 ? 15   LYS B O     1 
ATOM   3263  C  CB    . LYS J  3 15  ? 23.781  54.004  130.705 1.00 26.33 ? 15   LYS B CB    1 
ATOM   3264  C  CG    . LYS J  3 15  ? 23.244  52.702  131.278 1.00 27.69 ? 15   LYS B CG    1 
ATOM   3265  C  CD    . LYS J  3 15  ? 24.165  52.147  132.349 1.00 31.65 ? 15   LYS B CD    1 
ATOM   3266  C  CE    . LYS J  3 15  ? 23.622  50.831  132.896 1.00 34.99 ? 15   LYS B CE    1 
ATOM   3267  N  NZ    . LYS J  3 15  ? 24.658  50.118  133.702 1.00 36.64 ? 15   LYS B NZ    1 
ATOM   3268  N  N     . LEU J  3 16  ? 24.136  56.187  128.384 1.00 24.14 ? 16   LEU B N     1 
ATOM   3269  C  CA    . LEU J  3 16  ? 24.669  57.482  127.957 1.00 25.95 ? 16   LEU B CA    1 
ATOM   3270  C  C     . LEU J  3 16  ? 23.541  58.356  127.406 1.00 30.67 ? 16   LEU B C     1 
ATOM   3271  O  O     . LEU J  3 16  ? 23.494  59.567  127.644 1.00 26.94 ? 16   LEU B O     1 
ATOM   3272  C  CB    . LEU J  3 16  ? 25.739  57.284  126.884 1.00 24.98 ? 16   LEU B CB    1 
ATOM   3273  C  CG    . LEU J  3 16  ? 27.033  56.616  127.394 1.00 25.73 ? 16   LEU B CG    1 
ATOM   3274  C  CD1   . LEU J  3 16  ? 27.903  56.286  126.199 1.00 20.80 ? 16   LEU B CD1   1 
ATOM   3275  C  CD2   . LEU J  3 16  ? 27.764  57.539  128.372 1.00 24.95 ? 16   LEU B CD2   1 
ATOM   3276  N  N     . LEU J  3 17  ? 22.632  57.727  126.672 1.00 27.57 ? 17   LEU B N     1 
ATOM   3277  C  CA    . LEU J  3 17  ? 21.482  58.445  126.105 1.00 31.29 ? 17   LEU B CA    1 
ATOM   3278  C  C     . LEU J  3 17  ? 20.422  58.817  127.150 1.00 32.23 ? 17   LEU B C     1 
ATOM   3279  O  O     . LEU J  3 17  ? 19.958  59.958  127.189 1.00 32.05 ? 17   LEU B O     1 
ATOM   3280  C  CB    . LEU J  3 17  ? 20.840  57.596  125.007 1.00 28.12 ? 17   LEU B CB    1 
ATOM   3281  C  CG    . LEU J  3 17  ? 21.747  57.353  123.797 1.00 28.07 ? 17   LEU B CG    1 
ATOM   3282  C  CD1   . LEU J  3 17  ? 21.141  56.303  122.900 1.00 29.74 ? 17   LEU B CD1   1 
ATOM   3283  C  CD2   . LEU J  3 17  ? 21.996  58.645  123.045 1.00 29.65 ? 17   LEU B CD2   1 
ATOM   3284  N  N     . ASP J  3 18  ? 20.043  57.873  128.005 1.00 31.79 ? 18   ASP B N     1 
ATOM   3285  C  CA    . ASP J  3 18  ? 19.025  58.156  129.013 1.00 31.79 ? 18   ASP B CA    1 
ATOM   3286  C  C     . ASP J  3 18  ? 19.430  59.253  129.982 1.00 31.93 ? 18   ASP B C     1 
ATOM   3287  O  O     . ASP J  3 18  ? 18.576  59.957  130.526 1.00 31.83 ? 18   ASP B O     1 
ATOM   3288  C  CB    . ASP J  3 18  ? 18.666  56.901  129.820 1.00 38.29 ? 18   ASP B CB    1 
ATOM   3289  C  CG    . ASP J  3 18  ? 18.069  55.794  128.964 1.00 41.60 ? 18   ASP B CG    1 
ATOM   3290  O  OD1   . ASP J  3 18  ? 17.578  56.071  127.848 1.00 42.71 ? 18   ASP B OD1   1 
ATOM   3291  O  OD2   . ASP J  3 18  ? 18.076  54.631  129.426 1.00 45.56 ? 18   ASP B OD2   1 
ATOM   3292  N  N     . GLY J  3 19  ? 20.730  59.401  130.213 1.00 27.66 ? 19   GLY B N     1 
ATOM   3293  C  CA    . GLY J  3 19  ? 21.179  60.428  131.129 1.00 28.07 ? 19   GLY B CA    1 
ATOM   3294  C  C     . GLY J  3 19  ? 21.473  61.737  130.428 1.00 26.38 ? 19   GLY B C     1 
ATOM   3295  O  O     . GLY J  3 19  ? 21.944  62.683  131.052 1.00 28.95 ? 19   GLY B O     1 
ATOM   3296  N  N     . ASN J  3 20  ? 21.176  61.787  129.136 1.00 26.49 ? 20   ASN B N     1 
ATOM   3297  C  CA    . ASN J  3 20  ? 21.437  62.958  128.315 1.00 28.02 ? 20   ASN B CA    1 
ATOM   3298  C  C     . ASN J  3 20  ? 22.942  63.280  128.257 1.00 29.93 ? 20   ASN B C     1 
ATOM   3299  O  O     . ASN J  3 20  ? 23.334  64.420  127.971 1.00 26.79 ? 20   ASN B O     1 
ATOM   3300  C  CB    . ASN J  3 20  ? 20.669  64.185  128.835 1.00 31.10 ? 20   ASN B CB    1 
ATOM   3301  C  CG    . ASN J  3 20  ? 19.163  64.087  128.606 1.00 32.57 ? 20   ASN B CG    1 
ATOM   3302  O  OD1   . ASN J  3 20  ? 18.419  64.989  128.986 1.00 36.43 ? 20   ASN B OD1   1 
ATOM   3303  N  ND2   . ASN J  3 20  ? 18.715  63.005  127.984 1.00 29.30 ? 20   ASN B ND2   1 
ATOM   3304  N  N     . ILE J  3 21  ? 23.780  62.278  128.541 1.00 27.92 ? 21   ILE B N     1 
ATOM   3305  C  CA    . ILE J  3 21  ? 25.238  62.465  128.484 1.00 25.03 ? 21   ILE B CA    1 
ATOM   3306  C  C     . ILE J  3 21  ? 25.558  62.642  127.009 1.00 25.62 ? 21   ILE B C     1 
ATOM   3307  O  O     . ILE J  3 21  ? 26.278  63.570  126.615 1.00 23.91 ? 21   ILE B O     1 
ATOM   3308  C  CB    . ILE J  3 21  ? 26.003  61.233  129.023 1.00 24.60 ? 21   ILE B CB    1 
ATOM   3309  C  CG1   . ILE J  3 21  ? 25.423  60.790  130.382 1.00 27.23 ? 21   ILE B CG1   1 
ATOM   3310  C  CG2   . ILE J  3 21  ? 27.477  61.577  129.151 1.00 26.89 ? 21   ILE B CG2   1 
ATOM   3311  C  CD1   . ILE J  3 21  ? 25.419  61.864  131.451 1.00 30.97 ? 21   ILE B CD1   1 
ATOM   3312  N  N     . LEU J  3 22  ? 25.036  61.727  126.193 1.00 23.31 ? 22   LEU B N     1 
ATOM   3313  C  CA    . LEU J  3 22  ? 25.178  61.823  124.749 1.00 19.39 ? 22   LEU B CA    1 
ATOM   3314  C  C     . LEU J  3 22  ? 23.800  62.292  124.238 1.00 25.33 ? 22   LEU B C     1 
ATOM   3315  O  O     . LEU J  3 22  ? 22.808  61.566  124.366 1.00 25.78 ? 22   LEU B O     1 
ATOM   3316  C  CB    . LEU J  3 22  ? 25.500  60.470  124.120 1.00 21.10 ? 22   LEU B CB    1 
ATOM   3317  C  CG    . LEU J  3 22  ? 25.608  60.481  122.583 1.00 24.43 ? 22   LEU B CG    1 
ATOM   3318  C  CD1   . LEU J  3 22  ? 26.835  61.300  122.174 1.00 26.04 ? 22   LEU B CD1   1 
ATOM   3319  C  CD2   . LEU J  3 22  ? 25.725  59.057  122.022 1.00 26.51 ? 22   LEU B CD2   1 
ATOM   3320  N  N     . ALA J  3 23  ? 23.743  63.515  123.709 1.00 23.75 ? 23   ALA B N     1 
ATOM   3321  C  CA    . ALA J  3 23  ? 22.493  64.078  123.168 1.00 24.70 ? 23   ALA B CA    1 
ATOM   3322  C  C     . ALA J  3 23  ? 22.863  65.131  122.114 1.00 25.78 ? 23   ALA B C     1 
ATOM   3323  O  O     . ALA J  3 23  ? 24.044  65.311  121.801 1.00 26.34 ? 23   ALA B O     1 
ATOM   3324  C  CB    . ALA J  3 23  ? 21.672  64.697  124.287 1.00 22.51 ? 23   ALA B CB    1 
ATOM   3325  N  N     . THR J  3 24  ? 21.870  65.831  121.558 1.00 27.12 ? 24   THR B N     1 
ATOM   3326  C  CA    . THR J  3 24  ? 22.139  66.840  120.520 1.00 25.11 ? 24   THR B CA    1 
ATOM   3327  C  C     . THR J  3 24  ? 21.444  68.103  120.974 1.00 25.65 ? 24   THR B C     1 
ATOM   3328  O  O     . THR J  3 24  ? 20.305  68.027  121.440 1.00 24.72 ? 24   THR B O     1 
ATOM   3329  C  CB    . THR J  3 24  ? 21.518  66.435  119.157 1.00 26.87 ? 24   THR B CB    1 
ATOM   3330  O  OG1   . THR J  3 24  ? 21.932  65.105  118.820 1.00 26.75 ? 24   THR B OG1   1 
ATOM   3331  C  CG2   . THR J  3 24  ? 21.950  67.391  118.036 1.00 27.84 ? 24   THR B CG2   1 
ATOM   3332  N  N     . ASN J  3 25  ? 22.098  69.258  120.874 1.00 24.57 ? 25   ASN B N     1 
ATOM   3333  C  CA    . ASN J  3 25  ? 21.410  70.476  121.315 1.00 26.92 ? 25   ASN B CA    1 
ATOM   3334  C  C     . ASN J  3 25  ? 20.550  71.046  120.184 1.00 29.47 ? 25   ASN B C     1 
ATOM   3335  O  O     . ASN J  3 25  ? 20.542  70.497  119.084 1.00 26.43 ? 25   ASN B O     1 
ATOM   3336  C  CB    . ASN J  3 25  ? 22.392  71.531  121.879 1.00 25.13 ? 25   ASN B CB    1 
ATOM   3337  C  CG    . ASN J  3 25  ? 23.322  72.132  120.831 1.00 25.42 ? 25   ASN B CG    1 
ATOM   3338  O  OD1   . ASN J  3 25  ? 23.115  72.005  119.632 1.00 27.24 ? 25   ASN B OD1   1 
ATOM   3339  N  ND2   . ASN J  3 25  ? 24.366  72.816  121.306 1.00 25.88 ? 25   ASN B ND2   1 
ATOM   3340  N  N     . ASN J  3 26  ? 19.812  72.121  120.453 1.00 32.63 ? 26   ASN B N     1 
ATOM   3341  C  CA    . ASN J  3 26  ? 18.939  72.667  119.413 1.00 33.82 ? 26   ASN B CA    1 
ATOM   3342  C  C     . ASN J  3 26  ? 19.647  73.370  118.263 1.00 34.30 ? 26   ASN B C     1 
ATOM   3343  O  O     . ASN J  3 26  ? 18.986  73.908  117.365 1.00 31.88 ? 26   ASN B O     1 
ATOM   3344  C  CB    . ASN J  3 26  ? 17.839  73.569  120.007 1.00 37.05 ? 26   ASN B CB    1 
ATOM   3345  C  CG    . ASN J  3 26  ? 18.383  74.775  120.731 1.00 39.47 ? 26   ASN B CG    1 
ATOM   3346  O  OD1   . ASN J  3 26  ? 19.316  75.423  120.270 1.00 39.59 ? 26   ASN B OD1   1 
ATOM   3347  N  ND2   . ASN J  3 26  ? 17.781  75.096  121.870 1.00 45.15 ? 26   ASN B ND2   1 
ATOM   3348  N  N     . ARG J  3 27  ? 20.984  73.378  118.284 1.00 32.98 ? 27   ARG B N     1 
ATOM   3349  C  CA    . ARG J  3 27  ? 21.757  73.947  117.184 1.00 31.56 ? 27   ARG B CA    1 
ATOM   3350  C  C     . ARG J  3 27  ? 22.351  72.799  116.371 1.00 30.73 ? 27   ARG B C     1 
ATOM   3351  O  O     . ARG J  3 27  ? 23.121  73.020  115.440 1.00 34.13 ? 27   ARG B O     1 
ATOM   3352  C  CB    . ARG J  3 27  ? 22.895  74.846  117.677 1.00 33.76 ? 27   ARG B CB    1 
ATOM   3353  C  CG    . ARG J  3 27  ? 22.492  76.283  117.946 1.00 38.87 ? 27   ARG B CG    1 
ATOM   3354  C  CD    . ARG J  3 27  ? 21.864  76.409  119.309 1.00 44.18 ? 27   ARG B CD    1 
ATOM   3355  N  NE    . ARG J  3 27  ? 22.873  76.367  120.363 1.00 45.13 ? 27   ARG B NE    1 
ATOM   3356  C  CZ    . ARG J  3 27  ? 22.646  75.939  121.598 1.00 46.14 ? 27   ARG B CZ    1 
ATOM   3357  N  NH1   . ARG J  3 27  ? 21.441  75.505  121.947 1.00 43.95 ? 27   ARG B NH1   1 
ATOM   3358  N  NH2   . ARG J  3 27  ? 23.629  75.950  122.489 1.00 49.47 ? 27   ARG B NH2   1 
ATOM   3359  N  N     . GLY J  3 28  ? 22.022  71.564  116.751 1.00 30.19 ? 28   GLY B N     1 
ATOM   3360  C  CA    . GLY J  3 28  ? 22.516  70.423  116.005 1.00 26.26 ? 28   GLY B CA    1 
ATOM   3361  C  C     . GLY J  3 28  ? 23.864  69.869  116.438 1.00 27.54 ? 28   GLY B C     1 
ATOM   3362  O  O     . GLY J  3 28  ? 24.410  68.963  115.798 1.00 27.44 ? 28   GLY B O     1 
ATOM   3363  N  N     . VAL J  3 29  ? 24.408  70.408  117.519 1.00 25.57 ? 29   VAL B N     1 
ATOM   3364  C  CA    . VAL J  3 29  ? 25.707  69.936  118.002 1.00 23.96 ? 29   VAL B CA    1 
ATOM   3365  C  C     . VAL J  3 29  ? 25.546  68.741  118.946 1.00 21.62 ? 29   VAL B C     1 
ATOM   3366  O  O     . VAL J  3 29  ? 24.859  68.839  119.972 1.00 22.11 ? 29   VAL B O     1 
ATOM   3367  C  CB    . VAL J  3 29  ? 26.455  71.045  118.773 1.00 26.36 ? 29   VAL B CB    1 
ATOM   3368  C  CG1   . VAL J  3 29  ? 27.882  70.570  119.101 1.00 23.44 ? 29   VAL B CG1   1 
ATOM   3369  C  CG2   . VAL J  3 29  ? 26.514  72.327  117.933 1.00 28.13 ? 29   VAL B CG2   1 
ATOM   3370  N  N     . VAL J  3 30  ? 26.179  67.614  118.610 1.00 21.83 ? 30   VAL B N     1 
ATOM   3371  C  CA    . VAL J  3 30  ? 26.121  66.432  119.483 1.00 24.00 ? 30   VAL B CA    1 
ATOM   3372  C  C     . VAL J  3 30  ? 27.069  66.705  120.674 1.00 22.94 ? 30   VAL B C     1 
ATOM   3373  O  O     . VAL J  3 30  ? 28.133  67.309  120.494 1.00 24.50 ? 30   VAL B O     1 
ATOM   3374  C  CB    . VAL J  3 30  ? 26.507  65.155  118.701 1.00 24.37 ? 30   VAL B CB    1 
ATOM   3375  C  CG1   . VAL J  3 30  ? 26.457  63.912  119.631 1.00 21.40 ? 30   VAL B CG1   1 
ATOM   3376  C  CG2   . VAL J  3 30  ? 25.519  64.971  117.520 1.00 22.48 ? 30   VAL B CG2   1 
ATOM   3377  N  N     . SER J  3 31  ? 26.672  66.272  121.870 1.00 23.82 ? 31   SER B N     1 
ATOM   3378  C  CA    . SER J  3 31  ? 27.423  66.570  123.099 1.00 21.35 ? 31   SER B CA    1 
ATOM   3379  C  C     . SER J  3 31  ? 28.860  66.076  123.265 1.00 19.43 ? 31   SER B C     1 
ATOM   3380  O  O     . SER J  3 31  ? 29.490  66.426  124.257 1.00 23.82 ? 31   SER B O     1 
ATOM   3381  C  CB    . SER J  3 31  ? 26.607  66.174  124.334 1.00 23.16 ? 31   SER B CB    1 
ATOM   3382  O  OG    . SER J  3 31  ? 26.259  64.805  124.302 1.00 23.10 ? 31   SER B OG    1 
ATOM   3383  N  N     . ASN J  3 32  ? 29.361  65.245  122.362 1.00 19.16 ? 32   ASN B N     1 
ATOM   3384  C  CA    . ASN J  3 32  ? 30.770  64.852  122.465 1.00 21.81 ? 32   ASN B CA    1 
ATOM   3385  C  C     . ASN J  3 32  ? 31.555  65.523  121.326 1.00 23.43 ? 32   ASN B C     1 
ATOM   3386  O  O     . ASN J  3 32  ? 32.739  65.258  121.130 1.00 22.55 ? 32   ASN B O     1 
ATOM   3387  C  CB    . ASN J  3 32  ? 30.944  63.317  122.444 1.00 21.11 ? 32   ASN B CB    1 
ATOM   3388  C  CG    . ASN J  3 32  ? 30.447  62.678  121.153 1.00 24.53 ? 32   ASN B CG    1 
ATOM   3389  O  OD1   . ASN J  3 32  ? 29.527  63.192  120.502 1.00 22.73 ? 32   ASN B OD1   1 
ATOM   3390  N  ND2   . ASN J  3 32  ? 31.019  61.535  120.796 1.00 25.98 ? 32   ASN B ND2   1 
ATOM   3391  N  N     . ALA J  3 33  ? 30.893  66.408  120.579 1.00 21.15 ? 33   ALA B N     1 
ATOM   3392  C  CA    . ALA J  3 33  ? 31.551  67.109  119.480 1.00 22.87 ? 33   ALA B CA    1 
ATOM   3393  C  C     . ALA J  3 33  ? 32.189  68.421  119.928 1.00 22.71 ? 33   ALA B C     1 
ATOM   3394  O  O     . ALA J  3 33  ? 31.904  68.924  121.013 1.00 25.15 ? 33   ALA B O     1 
ATOM   3395  C  CB    . ALA J  3 33  ? 30.524  67.425  118.359 1.00 25.66 ? 33   ALA B CB    1 
ATOM   3396  N  N     . ASP J  3 34  ? 33.052  68.950  119.072 1.00 22.43 ? 34   ASP B N     1 
ATOM   3397  C  CA    . ASP J  3 34  ? 33.696  70.256  119.237 1.00 22.78 ? 34   ASP B CA    1 
ATOM   3398  C  C     . ASP J  3 34  ? 32.887  71.031  118.189 1.00 24.31 ? 34   ASP B C     1 
ATOM   3399  O  O     . ASP J  3 34  ? 33.146  70.897  116.993 1.00 22.87 ? 34   ASP B O     1 
ATOM   3400  C  CB    . ASP J  3 34  ? 35.166  70.193  118.813 1.00 24.81 ? 34   ASP B CB    1 
ATOM   3401  C  CG    . ASP J  3 34  ? 35.836  71.564  118.778 1.00 23.47 ? 34   ASP B CG    1 
ATOM   3402  O  OD1   . ASP J  3 34  ? 35.152  72.590  119.019 1.00 23.08 ? 34   ASP B OD1   1 
ATOM   3403  O  OD2   . ASP J  3 34  ? 37.051  71.606  118.500 1.00 24.53 ? 34   ASP B OD2   1 
ATOM   3404  N  N     . GLY J  3 35  ? 31.897  71.789  118.651 1.00 25.31 ? 35   GLY B N     1 
ATOM   3405  C  CA    . GLY J  3 35  ? 31.012  72.518  117.747 1.00 28.35 ? 35   GLY B CA    1 
ATOM   3406  C  C     . GLY J  3 35  ? 31.646  73.425  116.714 1.00 32.17 ? 35   GLY B C     1 
ATOM   3407  O  O     . GLY J  3 35  ? 31.033  73.729  115.691 1.00 35.74 ? 35   GLY B O     1 
ATOM   3408  N  N     . SER J  3 36  ? 32.873  73.856  116.978 1.00 32.30 ? 36   SER B N     1 
ATOM   3409  C  CA    . SER J  3 36  ? 33.608  74.764  116.094 1.00 32.84 ? 36   SER B CA    1 
ATOM   3410  C  C     . SER J  3 36  ? 34.312  74.034  114.958 1.00 33.63 ? 36   SER B C     1 
ATOM   3411  O  O     . SER J  3 36  ? 34.869  74.656  114.054 1.00 36.80 ? 36   SER B O     1 
ATOM   3412  C  CB    . SER J  3 36  ? 34.681  75.495  116.915 1.00 30.81 ? 36   SER B CB    1 
ATOM   3413  O  OG    . SER J  3 36  ? 35.729  74.585  117.270 1.00 33.59 ? 36   SER B OG    1 
ATOM   3414  N  N     . ASN J  3 37  ? 34.299  72.711  115.023 1.00 30.73 ? 37   ASN B N     1 
ATOM   3415  C  CA    . ASN J  3 37  ? 35.001  71.870  114.073 1.00 29.16 ? 37   ASN B CA    1 
ATOM   3416  C  C     . ASN J  3 37  ? 34.005  71.108  113.197 1.00 30.85 ? 37   ASN B C     1 
ATOM   3417  O  O     . ASN J  3 37  ? 33.332  70.191  113.667 1.00 29.73 ? 37   ASN B O     1 
ATOM   3418  C  CB    . ASN J  3 37  ? 35.884  70.901  114.885 1.00 30.98 ? 37   ASN B CB    1 
ATOM   3419  C  CG    . ASN J  3 37  ? 36.721  69.965  114.027 1.00 32.54 ? 37   ASN B CG    1 
ATOM   3420  O  OD1   . ASN J  3 37  ? 36.356  69.625  112.919 1.00 31.47 ? 37   ASN B OD1   1 
ATOM   3421  N  ND2   . ASN J  3 37  ? 37.855  69.509  114.580 1.00 39.04 ? 37   ASN B ND2   1 
ATOM   3422  N  N     . THR J  3 38  ? 33.937  71.472  111.917 1.00 31.21 ? 38   THR B N     1 
ATOM   3423  C  CA    . THR J  3 38  ? 32.998  70.828  110.996 1.00 29.33 ? 38   THR B CA    1 
ATOM   3424  C  C     . THR J  3 38  ? 33.117  69.306  110.928 1.00 27.66 ? 38   THR B C     1 
ATOM   3425  O  O     . THR J  3 38  ? 32.108  68.584  110.931 1.00 26.48 ? 38   THR B O     1 
ATOM   3426  C  CB    . THR J  3 38  ? 33.144  71.417  109.590 1.00 28.43 ? 38   THR B CB    1 
ATOM   3427  O  OG1   . THR J  3 38  ? 32.933  72.834  109.663 1.00 34.57 ? 38   THR B OG1   1 
ATOM   3428  C  CG2   . THR J  3 38  ? 32.118  70.794  108.641 1.00 29.44 ? 38   THR B CG2   1 
ATOM   3429  N  N     . ARG J  3 39  ? 34.346  68.806  110.883 1.00 28.24 ? 39   ARG B N     1 
ATOM   3430  C  CA    . ARG J  3 39  ? 34.546  67.368  110.831 1.00 30.66 ? 39   ARG B CA    1 
ATOM   3431  C  C     . ARG J  3 39  ? 34.094  66.723  112.136 1.00 28.18 ? 39   ARG B C     1 
ATOM   3432  O  O     . ARG J  3 39  ? 33.457  65.674  112.115 1.00 25.68 ? 39   ARG B O     1 
ATOM   3433  C  CB    . ARG J  3 39  ? 36.013  67.045  110.543 1.00 35.95 ? 39   ARG B CB    1 
ATOM   3434  C  CG    . ARG J  3 39  ? 36.456  67.414  109.131 1.00 41.08 ? 39   ARG B CG    1 
ATOM   3435  C  CD    . ARG J  3 39  ? 37.398  66.355  108.568 1.00 43.70 ? 39   ARG B CD    1 
ATOM   3436  N  NE    . ARG J  3 39  ? 37.807  66.631  107.192 1.00 47.67 ? 39   ARG B NE    1 
ATOM   3437  C  CZ    . ARG J  3 39  ? 38.621  67.622  106.842 1.00 49.59 ? 39   ARG B CZ    1 
ATOM   3438  N  NH1   . ARG J  3 39  ? 39.118  68.433  107.769 1.00 49.69 ? 39   ARG B NH1   1 
ATOM   3439  N  NH2   . ARG J  3 39  ? 38.937  67.805  105.566 1.00 49.07 ? 39   ARG B NH2   1 
ATOM   3440  N  N     . SER J  3 40  ? 34.411  67.355  113.268 1.00 28.20 ? 40   SER B N     1 
ATOM   3441  C  CA    . SER J  3 40  ? 33.985  66.825  114.561 1.00 26.80 ? 40   SER B CA    1 
ATOM   3442  C  C     . SER J  3 40  ? 32.445  66.822  114.633 1.00 24.06 ? 40   SER B C     1 
ATOM   3443  O  O     . SER J  3 40  ? 31.824  65.823  114.979 1.00 24.41 ? 40   SER B O     1 
ATOM   3444  C  CB    . SER J  3 40  ? 34.554  67.674  115.700 1.00 23.14 ? 40   SER B CB    1 
ATOM   3445  O  OG    . SER J  3 40  ? 34.145  67.143  116.954 1.00 24.38 ? 40   SER B OG    1 
ATOM   3446  N  N     . PHE J  3 41  ? 31.839  67.955  114.294 1.00 23.28 ? 41   PHE B N     1 
ATOM   3447  C  CA    . PHE J  3 41  ? 30.380  68.092  114.294 1.00 24.04 ? 41   PHE B CA    1 
ATOM   3448  C  C     . PHE J  3 41  ? 29.718  66.962  113.468 1.00 23.34 ? 41   PHE B C     1 
ATOM   3449  O  O     . PHE J  3 41  ? 28.796  66.275  113.926 1.00 23.61 ? 41   PHE B O     1 
ATOM   3450  C  CB    . PHE J  3 41  ? 30.046  69.478  113.692 1.00 26.23 ? 41   PHE B CB    1 
ATOM   3451  C  CG    . PHE J  3 41  ? 28.557  69.797  113.600 1.00 24.69 ? 41   PHE B CG    1 
ATOM   3452  C  CD1   . PHE J  3 41  ? 27.928  70.566  114.578 1.00 26.91 ? 41   PHE B CD1   1 
ATOM   3453  C  CD2   . PHE J  3 41  ? 27.810  69.369  112.506 1.00 28.49 ? 41   PHE B CD2   1 
ATOM   3454  C  CE1   . PHE J  3 41  ? 26.561  70.910  114.467 1.00 27.82 ? 41   PHE B CE1   1 
ATOM   3455  C  CE2   . PHE J  3 41  ? 26.452  69.707  112.388 1.00 25.57 ? 41   PHE B CE2   1 
ATOM   3456  C  CZ    . PHE J  3 41  ? 25.837  70.476  113.370 1.00 24.65 ? 41   PHE B CZ    1 
ATOM   3457  N  N     . ASN J  3 42  ? 30.211  66.752  112.262 1.00 25.76 ? 42   ASN B N     1 
ATOM   3458  C  CA    . ASN J  3 42  ? 29.626  65.744  111.388 1.00 26.90 ? 42   ASN B CA    1 
ATOM   3459  C  C     . ASN J  3 42  ? 29.846  64.319  111.854 1.00 27.86 ? 42   ASN B C     1 
ATOM   3460  O  O     . ASN J  3 42  ? 28.917  63.513  111.825 1.00 26.63 ? 42   ASN B O     1 
ATOM   3461  C  CB    . ASN J  3 42  ? 30.144  65.915  109.963 1.00 27.35 ? 42   ASN B CB    1 
ATOM   3462  C  CG    . ASN J  3 42  ? 29.644  67.206  109.308 1.00 33.67 ? 42   ASN B CG    1 
ATOM   3463  O  OD1   . ASN J  3 42  ? 28.539  67.676  109.597 1.00 36.15 ? 42   ASN B OD1   1 
ATOM   3464  N  ND2   . ASN J  3 42  ? 30.454  67.774  108.430 1.00 34.00 ? 42   ASN B ND2   1 
ATOM   3465  N  N     . ILE J  3 43  ? 31.062  64.003  112.300 1.00 29.04 ? 43   ILE B N     1 
ATOM   3466  C  CA    . ILE J  3 43  ? 31.334  62.652  112.774 1.00 27.14 ? 43   ILE B CA    1 
ATOM   3467  C  C     . ILE J  3 43  ? 30.468  62.350  113.983 1.00 23.29 ? 43   ILE B C     1 
ATOM   3468  O  O     . ILE J  3 43  ? 29.831  61.291  114.051 1.00 26.24 ? 43   ILE B O     1 
ATOM   3469  C  CB    . ILE J  3 43  ? 32.832  62.459  113.141 1.00 27.61 ? 43   ILE B CB    1 
ATOM   3470  C  CG1   . ILE J  3 43  ? 33.692  62.484  111.873 1.00 28.40 ? 43   ILE B CG1   1 
ATOM   3471  C  CG2   . ILE J  3 43  ? 33.016  61.152  113.886 1.00 25.53 ? 43   ILE B CG2   1 
ATOM   3472  C  CD1   . ILE J  3 43  ? 35.181  62.716  112.139 1.00 33.97 ? 43   ILE B CD1   1 
ATOM   3473  N  N     . ALA J  3 44  ? 30.420  63.282  114.938 1.00 23.14 ? 44   ALA B N     1 
ATOM   3474  C  CA    . ALA J  3 44  ? 29.607  63.066  116.126 1.00 21.18 ? 44   ALA B CA    1 
ATOM   3475  C  C     . ALA J  3 44  ? 28.127  62.877  115.774 1.00 23.95 ? 44   ALA B C     1 
ATOM   3476  O  O     . ALA J  3 44  ? 27.459  62.074  116.393 1.00 23.78 ? 44   ALA B O     1 
ATOM   3477  C  CB    . ALA J  3 44  ? 29.759  64.212  117.099 1.00 20.86 ? 44   ALA B CB    1 
ATOM   3478  N  N     . LYS J  3 45  ? 27.617  63.642  114.807 1.00 26.21 ? 45   LYS B N     1 
ATOM   3479  C  CA    . LYS J  3 45  ? 26.217  63.490  114.404 1.00 27.70 ? 45   LYS B CA    1 
ATOM   3480  C  C     . LYS J  3 45  ? 26.005  62.124  113.767 1.00 26.93 ? 45   LYS B C     1 
ATOM   3481  O  O     . LYS J  3 45  ? 25.018  61.457  114.052 1.00 27.64 ? 45   LYS B O     1 
ATOM   3482  C  CB    . LYS J  3 45  ? 25.786  64.557  113.390 1.00 33.14 ? 45   LYS B CB    1 
ATOM   3483  C  CG    . LYS J  3 45  ? 24.318  64.357  112.955 1.00 37.68 ? 45   LYS B CG    1 
ATOM   3484  C  CD    . LYS J  3 45  ? 23.799  65.453  112.066 1.00 46.89 ? 45   LYS B CD    1 
ATOM   3485  C  CE    . LYS J  3 45  ? 22.282  65.336  111.921 1.00 49.55 ? 45   LYS B CE    1 
ATOM   3486  N  NZ    . LYS J  3 45  ? 21.692  66.516  111.221 1.00 54.90 ? 45   LYS B NZ    1 
ATOM   3487  N  N     . GLY J  3 46  ? 26.929  61.725  112.902 1.00 25.78 ? 46   GLY B N     1 
ATOM   3488  C  CA    . GLY J  3 46  ? 26.821  60.424  112.252 1.00 29.01 ? 46   GLY B CA    1 
ATOM   3489  C  C     . GLY J  3 46  ? 26.752  59.306  113.284 1.00 31.67 ? 46   GLY B C     1 
ATOM   3490  O  O     . GLY J  3 46  ? 25.909  58.409  113.212 1.00 29.89 ? 46   GLY B O     1 
ATOM   3491  N  N     . ILE J  3 47  ? 27.637  59.356  114.273 1.00 29.76 ? 47   ILE B N     1 
ATOM   3492  C  CA    . ILE J  3 47  ? 27.623  58.344  115.320 1.00 25.84 ? 47   ILE B CA    1 
ATOM   3493  C  C     . ILE J  3 47  ? 26.321  58.372  116.137 1.00 26.29 ? 47   ILE B C     1 
ATOM   3494  O  O     . ILE J  3 47  ? 25.731  57.322  116.424 1.00 25.45 ? 47   ILE B O     1 
ATOM   3495  C  CB    . ILE J  3 47  ? 28.847  58.537  116.270 1.00 26.23 ? 47   ILE B CB    1 
ATOM   3496  C  CG1   . ILE J  3 47  ? 30.143  58.237  115.510 1.00 26.96 ? 47   ILE B CG1   1 
ATOM   3497  C  CG2   . ILE J  3 47  ? 28.695  57.664  117.508 1.00 22.62 ? 47   ILE B CG2   1 
ATOM   3498  C  CD1   . ILE J  3 47  ? 31.414  58.593  116.305 1.00 24.53 ? 47   ILE B CD1   1 
ATOM   3499  N  N     . ALA J  3 48  ? 25.865  59.568  116.514 1.00 25.05 ? 48   ALA B N     1 
ATOM   3500  C  CA    . ALA J  3 48  ? 24.642  59.687  117.310 1.00 26.99 ? 48   ALA B CA    1 
ATOM   3501  C  C     . ALA J  3 48  ? 23.445  59.048  116.588 1.00 26.31 ? 48   ALA B C     1 
ATOM   3502  O  O     . ALA J  3 48  ? 22.587  58.422  117.201 1.00 30.19 ? 48   ALA B O     1 
ATOM   3503  C  CB    . ALA J  3 48  ? 24.353  61.159  117.601 1.00 28.53 ? 48   ALA B CB    1 
ATOM   3504  N  N     . ASP J  3 49  ? 23.394  59.224  115.282 1.00 29.53 ? 49   ASP B N     1 
ATOM   3505  C  CA    . ASP J  3 49  ? 22.296  58.648  114.527 1.00 32.31 ? 49   ASP B CA    1 
ATOM   3506  C  C     . ASP J  3 49  ? 22.350  57.123  114.592 1.00 31.65 ? 49   ASP B C     1 
ATOM   3507  O  O     . ASP J  3 49  ? 21.326  56.463  114.785 1.00 27.11 ? 49   ASP B O     1 
ATOM   3508  C  CB    . ASP J  3 49  ? 22.335  59.124  113.075 1.00 30.57 ? 49   ASP B CB    1 
ATOM   3509  C  CG    . ASP J  3 49  ? 21.872  60.568  112.915 1.00 34.54 ? 49   ASP B CG    1 
ATOM   3510  O  OD1   . ASP J  3 49  ? 21.239  61.122  113.849 1.00 32.35 ? 49   ASP B OD1   1 
ATOM   3511  O  OD2   . ASP J  3 49  ? 22.133  61.142  111.840 1.00 34.17 ? 49   ASP B OD2   1 
ATOM   3512  N  N     . LEU J  3 50  ? 23.550  56.570  114.461 1.00 31.87 ? 50   LEU B N     1 
ATOM   3513  C  CA    . LEU J  3 50  ? 23.716  55.120  114.500 1.00 33.44 ? 50   LEU B CA    1 
ATOM   3514  C  C     . LEU J  3 50  ? 23.386  54.507  115.841 1.00 32.29 ? 50   LEU B C     1 
ATOM   3515  O  O     . LEU J  3 50  ? 23.066  53.317  115.923 1.00 36.24 ? 50   LEU B O     1 
ATOM   3516  C  CB    . LEU J  3 50  ? 25.129  54.742  114.068 1.00 34.90 ? 50   LEU B CB    1 
ATOM   3517  C  CG    . LEU J  3 50  ? 25.323  54.980  112.570 1.00 36.71 ? 50   LEU B CG    1 
ATOM   3518  C  CD1   . LEU J  3 50  ? 26.743  54.669  112.152 1.00 33.54 ? 50   LEU B CD1   1 
ATOM   3519  C  CD2   . LEU J  3 50  ? 24.320  54.099  111.804 1.00 37.09 ? 50   LEU B CD2   1 
ATOM   3520  N  N     . LEU J  3 51  ? 23.448  55.311  116.897 1.00 29.54 ? 51   LEU B N     1 
ATOM   3521  C  CA    . LEU J  3 51  ? 23.101  54.835  118.222 1.00 29.93 ? 51   LEU B CA    1 
ATOM   3522  C  C     . LEU J  3 51  ? 21.630  55.161  118.455 1.00 28.70 ? 51   LEU B C     1 
ATOM   3523  O  O     . LEU J  3 51  ? 21.092  54.910  119.528 1.00 33.13 ? 51   LEU B O     1 
ATOM   3524  C  CB    . LEU J  3 51  ? 23.976  55.516  119.283 1.00 29.92 ? 51   LEU B CB    1 
ATOM   3525  C  CG    . LEU J  3 51  ? 25.494  55.296  119.144 1.00 35.17 ? 51   LEU B CG    1 
ATOM   3526  C  CD1   . LEU J  3 51  ? 26.187  55.803  120.402 1.00 33.82 ? 51   LEU B CD1   1 
ATOM   3527  C  CD2   . LEU J  3 51  ? 25.801  53.826  118.947 1.00 33.28 ? 51   LEU B CD2   1 
ATOM   3528  N  N     . HIS J  3 52  ? 20.989  55.721  117.428 1.00 33.53 ? 52   HIS B N     1 
ATOM   3529  C  CA    . HIS J  3 52  ? 19.570  56.091  117.477 1.00 32.36 ? 52   HIS B CA    1 
ATOM   3530  C  C     . HIS J  3 52  ? 19.217  57.140  118.524 1.00 30.55 ? 52   HIS B C     1 
ATOM   3531  O  O     . HIS J  3 52  ? 18.159  57.077  119.157 1.00 32.03 ? 52   HIS B O     1 
ATOM   3532  C  CB    . HIS J  3 52  ? 18.698  54.843  117.682 1.00 37.71 ? 52   HIS B CB    1 
ATOM   3533  C  CG    . HIS J  3 52  ? 18.803  53.856  116.563 1.00 43.31 ? 52   HIS B CG    1 
ATOM   3534  N  ND1   . HIS J  3 52  ? 18.604  54.206  115.244 1.00 46.90 ? 52   HIS B ND1   1 
ATOM   3535  C  CD2   . HIS J  3 52  ? 19.133  52.543  116.556 1.00 48.19 ? 52   HIS B CD2   1 
ATOM   3536  C  CE1   . HIS J  3 52  ? 18.808  53.153  114.474 1.00 49.52 ? 52   HIS B CE1   1 
ATOM   3537  N  NE2   . HIS J  3 52  ? 19.131  52.130  115.244 1.00 51.23 ? 52   HIS B NE2   1 
ATOM   3538  N  N     . SER J  3 53  ? 20.111  58.110  118.705 1.00 28.36 ? 53   SER B N     1 
ATOM   3539  C  CA    . SER J  3 53  ? 19.897  59.191  119.668 1.00 26.86 ? 53   SER B CA    1 
ATOM   3540  C  C     . SER J  3 53  ? 18.830  60.119  119.087 1.00 24.73 ? 53   SER B C     1 
ATOM   3541  O  O     . SER J  3 53  ? 18.899  60.475  117.913 1.00 26.42 ? 53   SER B O     1 
ATOM   3542  C  CB    . SER J  3 53  ? 21.192  59.980  119.851 1.00 25.60 ? 53   SER B CB    1 
ATOM   3543  O  OG    . SER J  3 53  ? 21.010  61.063  120.747 1.00 29.05 ? 53   SER B OG    1 
ATOM   3544  N  N     . GLU J  3 54  ? 17.853  60.494  119.904 1.00 25.65 ? 54   GLU B N     1 
ATOM   3545  C  CA    . GLU J  3 54  ? 16.803  61.385  119.425 1.00 25.89 ? 54   GLU B CA    1 
ATOM   3546  C  C     . GLU J  3 54  ? 16.538  62.540  120.377 1.00 28.87 ? 54   GLU B C     1 
ATOM   3547  O  O     . GLU J  3 54  ? 15.797  63.461  120.041 1.00 32.05 ? 54   GLU B O     1 
ATOM   3548  C  CB    . GLU J  3 54  ? 15.506  60.591  119.212 1.00 24.64 ? 54   GLU B CB    1 
ATOM   3549  C  CG    . GLU J  3 54  ? 15.604  59.590  118.082 1.00 23.58 ? 54   GLU B CG    1 
ATOM   3550  C  CD    . GLU J  3 54  ? 14.330  58.777  117.915 1.00 24.98 ? 54   GLU B CD    1 
ATOM   3551  O  OE1   . GLU J  3 54  ? 13.230  59.335  118.124 1.00 24.79 ? 54   GLU B OE1   1 
ATOM   3552  O  OE2   . GLU J  3 54  ? 14.437  57.598  117.559 1.00 25.88 ? 54   GLU B OE2   1 
ATOM   3553  N  N     . THR J  3 55  ? 17.133  62.505  121.563 1.00 25.98 ? 55   THR B N     1 
ATOM   3554  C  CA    . THR J  3 55  ? 16.912  63.557  122.544 1.00 26.98 ? 55   THR B CA    1 
ATOM   3555  C  C     . THR J  3 55  ? 17.609  64.872  122.215 1.00 28.36 ? 55   THR B C     1 
ATOM   3556  O  O     . THR J  3 55  ? 18.785  64.888  121.840 1.00 27.83 ? 55   THR B O     1 
ATOM   3557  C  CB    . THR J  3 55  ? 17.383  63.115  123.929 1.00 26.86 ? 55   THR B CB    1 
ATOM   3558  O  OG1   . THR J  3 55  ? 16.649  61.962  124.323 1.00 27.53 ? 55   THR B OG1   1 
ATOM   3559  C  CG2   . THR J  3 55  ? 17.165  64.222  124.977 1.00 27.87 ? 55   THR B CG2   1 
ATOM   3560  N  N     . VAL J  3 56  ? 16.860  65.967  122.336 1.00 27.18 ? 56   VAL B N     1 
ATOM   3561  C  CA    . VAL J  3 56  ? 17.393  67.306  122.123 1.00 26.21 ? 56   VAL B CA    1 
ATOM   3562  C  C     . VAL J  3 56  ? 17.498  67.947  123.496 1.00 27.76 ? 56   VAL B C     1 
ATOM   3563  O  O     . VAL J  3 56  ? 16.507  68.048  124.213 1.00 28.17 ? 56   VAL B O     1 
ATOM   3564  C  CB    . VAL J  3 56  ? 16.449  68.166  121.253 1.00 25.45 ? 56   VAL B CB    1 
ATOM   3565  C  CG1   . VAL J  3 56  ? 17.050  69.563  121.071 1.00 26.23 ? 56   VAL B CG1   1 
ATOM   3566  C  CG2   . VAL J  3 56  ? 16.251  67.496  119.901 1.00 23.83 ? 56   VAL B CG2   1 
ATOM   3567  N  N     . SER J  3 57  ? 18.705  68.366  123.872 1.00 24.64 ? 57   SER B N     1 
ATOM   3568  C  CA    . SER J  3 57  ? 18.917  68.998  125.165 1.00 26.12 ? 57   SER B CA    1 
ATOM   3569  C  C     . SER J  3 57  ? 20.255  69.722  125.116 1.00 26.03 ? 57   SER B C     1 
ATOM   3570  O  O     . SER J  3 57  ? 21.085  69.436  124.253 1.00 26.85 ? 57   SER B O     1 
ATOM   3571  C  CB    . SER J  3 57  ? 18.940  67.960  126.279 1.00 29.89 ? 57   SER B CB    1 
ATOM   3572  O  OG    . SER J  3 57  ? 19.995  67.042  126.083 1.00 38.19 ? 57   SER B OG    1 
ATOM   3573  N  N     . GLU J  3 58  ? 20.455  70.655  126.036 1.00 25.54 ? 58   GLU B N     1 
ATOM   3574  C  CA    . GLU J  3 58  ? 21.710  71.378  126.079 1.00 26.71 ? 58   GLU B CA    1 
ATOM   3575  C  C     . GLU J  3 58  ? 22.811  70.435  126.570 1.00 25.90 ? 58   GLU B C     1 
ATOM   3576  O  O     . GLU J  3 58  ? 22.558  69.495  127.331 1.00 26.75 ? 58   GLU B O     1 
ATOM   3577  C  CB    . GLU J  3 58  ? 21.608  72.576  127.023 1.00 28.31 ? 58   GLU B CB    1 
ATOM   3578  C  CG    . GLU J  3 58  ? 20.778  73.743  126.472 1.00 33.05 ? 58   GLU B CG    1 
ATOM   3579  C  CD    . GLU J  3 58  ? 21.326  74.283  125.160 1.00 35.85 ? 58   GLU B CD    1 
ATOM   3580  O  OE1   . GLU J  3 58  ? 22.521  74.642  125.108 1.00 40.46 ? 58   GLU B OE1   1 
ATOM   3581  O  OE2   . GLU J  3 58  ? 20.566  74.359  124.172 1.00 40.28 ? 58   GLU B OE2   1 
ATOM   3582  N  N     . ARG J  3 59  ? 24.028  70.705  126.122 1.00 24.02 ? 59   ARG B N     1 
ATOM   3583  C  CA    . ARG J  3 59  ? 25.194  69.918  126.529 1.00 22.90 ? 59   ARG B CA    1 
ATOM   3584  C  C     . ARG J  3 59  ? 25.288  69.970  128.051 1.00 23.27 ? 59   ARG B C     1 
ATOM   3585  O  O     . ARG J  3 59  ? 25.028  71.010  128.662 1.00 24.30 ? 59   ARG B O     1 
ATOM   3586  C  CB    . ARG J  3 59  ? 26.452  70.531  125.907 1.00 23.17 ? 59   ARG B CB    1 
ATOM   3587  C  CG    . ARG J  3 59  ? 27.738  69.746  126.216 1.00 24.00 ? 59   ARG B CG    1 
ATOM   3588  C  CD    . ARG J  3 59  ? 29.007  70.383  125.600 1.00 24.92 ? 59   ARG B CD    1 
ATOM   3589  N  NE    . ARG J  3 59  ? 28.947  70.436  124.151 1.00 28.09 ? 59   ARG B NE    1 
ATOM   3590  C  CZ    . ARG J  3 59  ? 29.803  69.840  123.330 1.00 25.06 ? 59   ARG B CZ    1 
ATOM   3591  N  NH1   . ARG J  3 59  ? 30.827  69.120  123.802 1.00 25.37 ? 59   ARG B NH1   1 
ATOM   3592  N  NH2   . ARG J  3 59  ? 29.646  69.983  122.024 1.00 25.45 ? 59   ARG B NH2   1 
ATOM   3593  N  N     . LEU J  3 60  ? 25.645  68.855  128.683 1.00 24.25 ? 60   LEU B N     1 
ATOM   3594  C  CA    . LEU J  3 60  ? 25.766  68.854  130.134 1.00 22.64 ? 60   LEU B CA    1 
ATOM   3595  C  C     . LEU J  3 60  ? 27.098  69.498  130.543 1.00 22.62 ? 60   LEU B C     1 
ATOM   3596  O  O     . LEU J  3 60  ? 28.017  69.555  129.737 1.00 21.06 ? 60   LEU B O     1 
ATOM   3597  C  CB    . LEU J  3 60  ? 25.753  67.418  130.649 1.00 24.97 ? 60   LEU B CB    1 
ATOM   3598  C  CG    . LEU J  3 60  ? 24.498  66.585  130.398 1.00 29.42 ? 60   LEU B CG    1 
ATOM   3599  C  CD1   . LEU J  3 60  ? 24.665  65.207  131.055 1.00 28.61 ? 60   LEU B CD1   1 
ATOM   3600  C  CD2   . LEU J  3 60  ? 23.287  67.330  130.965 1.00 30.26 ? 60   LEU B CD2   1 
ATOM   3601  N  N     . PRO J  3 61  ? 27.204  70.008  131.789 1.00 23.91 ? 61   PRO B N     1 
ATOM   3602  C  CA    . PRO J  3 61  ? 28.482  70.605  132.203 1.00 20.52 ? 61   PRO B CA    1 
ATOM   3603  C  C     . PRO J  3 61  ? 29.553  69.518  132.041 1.00 19.95 ? 61   PRO B C     1 
ATOM   3604  O  O     . PRO J  3 61  ? 29.279  68.342  132.232 1.00 22.11 ? 61   PRO B O     1 
ATOM   3605  C  CB    . PRO J  3 61  ? 28.255  70.950  133.679 1.00 21.32 ? 61   PRO B CB    1 
ATOM   3606  C  CG    . PRO J  3 61  ? 26.756  71.290  133.704 1.00 22.70 ? 61   PRO B CG    1 
ATOM   3607  C  CD    . PRO J  3 61  ? 26.139  70.243  132.785 1.00 22.25 ? 61   PRO B CD    1 
ATOM   3608  N  N     . GLY J  3 62  ? 30.776  69.908  131.705 1.00 19.09 ? 62   GLY B N     1 
ATOM   3609  C  CA    . GLY J  3 62  ? 31.831  68.918  131.540 1.00 19.51 ? 62   GLY B CA    1 
ATOM   3610  C  C     . GLY J  3 62  ? 32.098  68.094  132.792 1.00 17.74 ? 62   GLY B C     1 
ATOM   3611  O  O     . GLY J  3 62  ? 32.513  66.952  132.700 1.00 19.13 ? 62   GLY B O     1 
ATOM   3612  N  N     . GLN J  3 63  ? 31.902  68.673  133.967 1.00 17.48 ? 63   GLN B N     1 
ATOM   3613  C  CA    . GLN J  3 63  ? 32.138  67.926  135.193 1.00 15.61 ? 63   GLN B CA    1 
ATOM   3614  C  C     . GLN J  3 63  ? 31.122  66.786  135.281 1.00 18.51 ? 63   GLN B C     1 
ATOM   3615  O  O     . GLN J  3 63  ? 31.429  65.693  135.760 1.00 17.78 ? 63   GLN B O     1 
ATOM   3616  C  CB    . GLN J  3 63  ? 31.997  68.839  136.422 1.00 20.15 ? 63   GLN B CB    1 
ATOM   3617  C  CG    . GLN J  3 63  ? 32.951  70.042  136.453 1.00 18.21 ? 63   GLN B CG    1 
ATOM   3618  C  CD    . GLN J  3 63  ? 32.400  71.279  135.738 1.00 19.73 ? 63   GLN B CD    1 
ATOM   3619  O  OE1   . GLN J  3 63  ? 31.494  71.202  134.883 1.00 18.88 ? 63   GLN B OE1   1 
ATOM   3620  N  NE2   . GLN J  3 63  ? 32.955  72.431  136.078 1.00 19.29 ? 63   GLN B NE2   1 
ATOM   3621  N  N     . THR J  3 64  ? 29.903  67.064  134.832 1.00 19.99 ? 64   THR B N     1 
ATOM   3622  C  CA    . THR J  3 64  ? 28.831  66.080  134.858 1.00 18.54 ? 64   THR B CA    1 
ATOM   3623  C  C     . THR J  3 64  ? 29.043  64.947  133.877 1.00 19.77 ? 64   THR B C     1 
ATOM   3624  O  O     . THR J  3 64  ? 28.920  63.770  134.257 1.00 20.39 ? 64   THR B O     1 
ATOM   3625  C  CB    . THR J  3 64  ? 27.471  66.755  134.567 1.00 18.93 ? 64   THR B CB    1 
ATOM   3626  O  OG1   . THR J  3 64  ? 27.280  67.803  135.524 1.00 20.75 ? 64   THR B OG1   1 
ATOM   3627  C  CG2   . THR J  3 64  ? 26.321  65.747  134.674 1.00 19.50 ? 64   THR B CG2   1 
ATOM   3628  N  N     . SER J  3 65  ? 29.332  65.275  132.620 1.00 17.40 ? 65   SER B N     1 
ATOM   3629  C  CA    . SER J  3 65  ? 29.565  64.244  131.614 1.00 19.84 ? 65   SER B CA    1 
ATOM   3630  C  C     . SER J  3 65  ? 30.824  63.427  131.973 1.00 23.18 ? 65   SER B C     1 
ATOM   3631  O  O     . SER J  3 65  ? 30.866  62.205  131.793 1.00 20.16 ? 65   SER B O     1 
ATOM   3632  C  CB    . SER J  3 65  ? 29.709  64.873  130.213 1.00 19.48 ? 65   SER B CB    1 
ATOM   3633  O  OG    . SER J  3 65  ? 30.773  65.823  130.112 1.00 19.79 ? 65   SER B OG    1 
ATOM   3634  N  N     . GLY J  3 66  ? 31.841  64.101  132.499 1.00 20.38 ? 66   GLY B N     1 
ATOM   3635  C  CA    . GLY J  3 66  ? 33.051  63.388  132.875 1.00 17.26 ? 66   GLY B CA    1 
ATOM   3636  C  C     . GLY J  3 66  ? 32.788  62.311  133.927 1.00 19.71 ? 66   GLY B C     1 
ATOM   3637  O  O     . GLY J  3 66  ? 33.201  61.162  133.774 1.00 18.81 ? 66   GLY B O     1 
ATOM   3638  N  N     . ASN J  3 67  ? 32.108  62.687  135.005 1.00 19.69 ? 67   ASN B N     1 
ATOM   3639  C  CA    . ASN J  3 67  ? 31.784  61.753  136.077 1.00 19.13 ? 67   ASN B CA    1 
ATOM   3640  C  C     . ASN J  3 67  ? 30.830  60.661  135.606 1.00 22.57 ? 67   ASN B C     1 
ATOM   3641  O  O     . ASN J  3 67  ? 31.009  59.470  135.912 1.00 20.64 ? 67   ASN B O     1 
ATOM   3642  C  CB    . ASN J  3 67  ? 31.163  62.518  137.262 1.00 20.26 ? 67   ASN B CB    1 
ATOM   3643  C  CG    . ASN J  3 67  ? 30.758  61.597  138.406 1.00 22.20 ? 67   ASN B CG    1 
ATOM   3644  O  OD1   . ASN J  3 67  ? 29.564  61.352  138.646 1.00 29.29 ? 67   ASN B OD1   1 
ATOM   3645  N  ND2   . ASN J  3 67  ? 31.741  61.079  139.107 1.00 21.87 ? 67   ASN B ND2   1 
ATOM   3646  N  N     . ALA J  3 68  ? 29.825  61.052  134.827 1.00 19.48 ? 68   ALA B N     1 
ATOM   3647  C  CA    . ALA J  3 68  ? 28.838  60.085  134.362 1.00 21.97 ? 68   ALA B CA    1 
ATOM   3648  C  C     . ALA J  3 68  ? 29.489  59.066  133.448 1.00 19.79 ? 68   ALA B C     1 
ATOM   3649  O  O     . ALA J  3 68  ? 29.209  57.878  133.551 1.00 20.74 ? 68   ALA B O     1 
ATOM   3650  C  CB    . ALA J  3 68  ? 27.696  60.807  133.626 1.00 22.23 ? 68   ALA B CB    1 
ATOM   3651  N  N     . PHE J  3 69  ? 30.365  59.532  132.555 1.00 20.76 ? 69   PHE B N     1 
ATOM   3652  C  CA    . PHE J  3 69  ? 31.031  58.626  131.632 1.00 18.59 ? 69   PHE B CA    1 
ATOM   3653  C  C     . PHE J  3 69  ? 31.856  57.587  132.411 1.00 18.74 ? 69   PHE B C     1 
ATOM   3654  O  O     . PHE J  3 69  ? 31.863  56.400  132.058 1.00 19.21 ? 69   PHE B O     1 
ATOM   3655  C  CB    . PHE J  3 69  ? 31.917  59.424  130.657 1.00 19.06 ? 69   PHE B CB    1 
ATOM   3656  C  CG    . PHE J  3 69  ? 32.519  58.594  129.558 1.00 20.15 ? 69   PHE B CG    1 
ATOM   3657  C  CD1   . PHE J  3 69  ? 31.714  57.837  128.700 1.00 18.18 ? 69   PHE B CD1   1 
ATOM   3658  C  CD2   . PHE J  3 69  ? 33.904  58.576  129.364 1.00 20.86 ? 69   PHE B CD2   1 
ATOM   3659  C  CE1   . PHE J  3 69  ? 32.277  57.072  127.662 1.00 19.07 ? 69   PHE B CE1   1 
ATOM   3660  C  CE2   . PHE J  3 69  ? 34.466  57.813  128.324 1.00 16.69 ? 69   PHE B CE2   1 
ATOM   3661  C  CZ    . PHE J  3 69  ? 33.646  57.062  127.477 1.00 17.84 ? 69   PHE B CZ    1 
ATOM   3662  N  N     . GLU J  3 70  ? 32.535  58.031  133.469 1.00 19.26 ? 70   GLU B N     1 
ATOM   3663  C  CA    . GLU J  3 70  ? 33.316  57.118  134.308 1.00 18.47 ? 70   GLU B CA    1 
ATOM   3664  C  C     . GLU J  3 70  ? 32.403  56.052  134.910 1.00 18.78 ? 70   GLU B C     1 
ATOM   3665  O  O     . GLU J  3 70  ? 32.693  54.853  134.850 1.00 19.25 ? 70   GLU B O     1 
ATOM   3666  C  CB    . GLU J  3 70  ? 33.986  57.867  135.468 1.00 18.72 ? 70   GLU B CB    1 
ATOM   3667  C  CG    . GLU J  3 70  ? 35.172  58.743  135.076 1.00 20.95 ? 70   GLU B CG    1 
ATOM   3668  C  CD    . GLU J  3 70  ? 35.805  59.422  136.274 1.00 22.73 ? 70   GLU B CD    1 
ATOM   3669  O  OE1   . GLU J  3 70  ? 35.351  59.182  137.415 1.00 22.51 ? 70   GLU B OE1   1 
ATOM   3670  O  OE2   . GLU J  3 70  ? 36.765  60.196  136.078 1.00 22.82 ? 70   GLU B OE2   1 
ATOM   3671  N  N     . ALA J  3 71  ? 31.301  56.509  135.505 1.00 20.91 ? 71   ALA B N     1 
ATOM   3672  C  CA    . ALA J  3 71  ? 30.359  55.605  136.152 1.00 20.82 ? 71   ALA B CA    1 
ATOM   3673  C  C     . ALA J  3 71  ? 29.797  54.571  135.194 1.00 21.79 ? 71   ALA B C     1 
ATOM   3674  O  O     . ALA J  3 71  ? 29.732  53.374  135.509 1.00 20.09 ? 71   ALA B O     1 
ATOM   3675  C  CB    . ALA J  3 71  ? 29.215  56.413  136.799 1.00 22.12 ? 71   ALA B CB    1 
ATOM   3676  N  N     . ILE J  3 72  ? 29.371  55.037  134.027 1.00 19.34 ? 72   ILE B N     1 
ATOM   3677  C  CA    . ILE J  3 72  ? 28.801  54.154  133.019 1.00 22.25 ? 72   ILE B CA    1 
ATOM   3678  C  C     . ILE J  3 72  ? 29.815  53.155  132.457 1.00 21.65 ? 72   ILE B C     1 
ATOM   3679  O  O     . ILE J  3 72  ? 29.480  51.990  132.201 1.00 22.14 ? 72   ILE B O     1 
ATOM   3680  C  CB    . ILE J  3 72  ? 28.134  55.002  131.920 1.00 22.78 ? 72   ILE B CB    1 
ATOM   3681  C  CG1   . ILE J  3 72  ? 26.894  55.668  132.529 1.00 24.09 ? 72   ILE B CG1   1 
ATOM   3682  C  CG2   . ILE J  3 72  ? 27.755  54.156  130.740 1.00 21.88 ? 72   ILE B CG2   1 
ATOM   3683  C  CD1   . ILE J  3 72  ? 26.275  56.732  131.642 1.00 21.88 ? 72   ILE B CD1   1 
ATOM   3684  N  N     . CYS J  3 73  ? 31.057  53.589  132.270 1.00 17.67 ? 73   CYS B N     1 
ATOM   3685  C  CA    . CYS J  3 73  ? 32.093  52.666  131.788 1.00 18.87 ? 73   CYS B CA    1 
ATOM   3686  C  C     . CYS J  3 73  ? 32.362  51.610  132.878 1.00 17.11 ? 73   CYS B C     1 
ATOM   3687  O  O     . CYS J  3 73  ? 32.570  50.444  132.578 1.00 19.21 ? 73   CYS B O     1 
ATOM   3688  C  CB    . CYS J  3 73  ? 33.402  53.424  131.508 1.00 17.99 ? 73   CYS B CB    1 
ATOM   3689  S  SG    . CYS J  3 73  ? 33.457  54.396  129.982 1.00 20.68 ? 73   CYS B SG    1 
ATOM   3690  N  N     . SER J  3 74  ? 32.368  52.032  134.138 1.00 18.28 ? 74   SER B N     1 
ATOM   3691  C  CA    . SER J  3 74  ? 32.620  51.121  135.231 1.00 20.74 ? 74   SER B CA    1 
ATOM   3692  C  C     . SER J  3 74  ? 31.547  50.036  135.271 1.00 22.30 ? 74   SER B C     1 
ATOM   3693  O  O     . SER J  3 74  ? 31.851  48.840  135.400 1.00 21.03 ? 74   SER B O     1 
ATOM   3694  C  CB    . SER J  3 74  ? 32.643  51.887  136.549 1.00 21.99 ? 74   SER B CB    1 
ATOM   3695  O  OG    . SER J  3 74  ? 32.939  51.013  137.625 1.00 31.84 ? 74   SER B OG    1 
ATOM   3696  N  N     . GLU J  3 75  ? 30.286  50.453  135.154 1.00 21.38 ? 75   GLU B N     1 
ATOM   3697  C  CA    . GLU J  3 75  ? 29.185  49.486  135.178 1.00 22.10 ? 75   GLU B CA    1 
ATOM   3698  C  C     . GLU J  3 75  ? 29.271  48.469  134.030 1.00 21.34 ? 75   GLU B C     1 
ATOM   3699  O  O     . GLU J  3 75  ? 28.995  47.279  134.220 1.00 22.73 ? 75   GLU B O     1 
ATOM   3700  C  CB    . GLU J  3 75  ? 27.837  50.231  135.162 1.00 20.68 ? 75   GLU B CB    1 
ATOM   3701  C  CG    . GLU J  3 75  ? 27.688  51.152  136.354 1.00 26.67 ? 75   GLU B CG    1 
ATOM   3702  C  CD    . GLU J  3 75  ? 26.344  51.889  136.392 1.00 36.39 ? 75   GLU B CD    1 
ATOM   3703  O  OE1   . GLU J  3 75  ? 25.662  51.981  135.344 1.00 36.33 ? 75   GLU B OE1   1 
ATOM   3704  O  OE2   . GLU J  3 75  ? 25.996  52.382  137.483 1.00 39.25 ? 75   GLU B OE2   1 
ATOM   3705  N  N     . PHE J  3 76  ? 29.667  48.926  132.847 1.00 19.94 ? 76   PHE B N     1 
ATOM   3706  C  CA    . PHE J  3 76  ? 29.799  48.042  131.693 1.00 21.10 ? 76   PHE B CA    1 
ATOM   3707  C  C     . PHE J  3 76  ? 30.922  47.022  131.937 1.00 22.74 ? 76   PHE B C     1 
ATOM   3708  O  O     . PHE J  3 76  ? 30.751  45.828  131.717 1.00 22.20 ? 76   PHE B O     1 
ATOM   3709  C  CB    . PHE J  3 76  ? 30.117  48.863  130.433 1.00 21.18 ? 76   PHE B CB    1 
ATOM   3710  C  CG    . PHE J  3 76  ? 30.608  48.040  129.275 1.00 23.60 ? 76   PHE B CG    1 
ATOM   3711  C  CD1   . PHE J  3 76  ? 29.726  47.291  128.498 1.00 24.23 ? 76   PHE B CD1   1 
ATOM   3712  C  CD2   . PHE J  3 76  ? 31.975  47.968  128.980 1.00 24.90 ? 76   PHE B CD2   1 
ATOM   3713  C  CE1   . PHE J  3 76  ? 30.198  46.489  127.453 1.00 26.27 ? 76   PHE B CE1   1 
ATOM   3714  C  CE2   . PHE J  3 76  ? 32.446  47.165  127.935 1.00 25.14 ? 76   PHE B CE2   1 
ATOM   3715  C  CZ    . PHE J  3 76  ? 31.564  46.425  127.171 1.00 23.96 ? 76   PHE B CZ    1 
ATOM   3716  N  N     . VAL J  3 77  ? 32.076  47.496  132.386 1.00 22.34 ? 77   VAL B N     1 
ATOM   3717  C  CA    . VAL J  3 77  ? 33.194  46.580  132.620 1.00 20.49 ? 77   VAL B CA    1 
ATOM   3718  C  C     . VAL J  3 77  ? 32.840  45.544  133.687 1.00 21.38 ? 77   VAL B C     1 
ATOM   3719  O  O     . VAL J  3 77  ? 33.112  44.357  133.528 1.00 23.16 ? 77   VAL B O     1 
ATOM   3720  C  CB    . VAL J  3 77  ? 34.470  47.358  133.040 1.00 20.53 ? 77   VAL B CB    1 
ATOM   3721  C  CG1   . VAL J  3 77  ? 35.591  46.392  133.435 1.00 22.47 ? 77   VAL B CG1   1 
ATOM   3722  C  CG2   . VAL J  3 77  ? 34.955  48.203  131.866 1.00 24.47 ? 77   VAL B CG2   1 
ATOM   3723  N  N     . GLN J  3 78  ? 32.211  45.989  134.761 1.00 20.35 ? 78   GLN B N     1 
ATOM   3724  C  CA    . GLN J  3 78  ? 31.858  45.073  135.838 1.00 24.25 ? 78   GLN B CA    1 
ATOM   3725  C  C     . GLN J  3 78  ? 30.891  43.996  135.340 1.00 24.07 ? 78   GLN B C     1 
ATOM   3726  O  O     . GLN J  3 78  ? 31.100  42.803  135.562 1.00 25.04 ? 78   GLN B O     1 
ATOM   3727  C  CB    . GLN J  3 78  ? 31.249  45.870  136.995 1.00 25.34 ? 78   GLN B CB    1 
ATOM   3728  C  CG    . GLN J  3 78  ? 31.014  45.086  138.279 1.00 33.27 ? 78   GLN B CG    1 
ATOM   3729  C  CD    . GLN J  3 78  ? 29.839  44.137  138.183 1.00 40.67 ? 78   GLN B CD    1 
ATOM   3730  O  OE1   . GLN J  3 78  ? 28.803  44.465  137.591 1.00 43.40 ? 78   GLN B OE1   1 
ATOM   3731  N  NE2   . GLN J  3 78  ? 29.982  42.954  138.779 1.00 44.16 ? 78   GLN B NE2   1 
ATOM   3732  N  N     . SER J  3 79  ? 29.850  44.411  134.628 1.00 23.07 ? 79   SER B N     1 
ATOM   3733  C  CA    . SER J  3 79  ? 28.855  43.456  134.138 1.00 26.44 ? 79   SER B CA    1 
ATOM   3734  C  C     . SER J  3 79  ? 29.407  42.456  133.128 1.00 24.84 ? 79   SER B C     1 
ATOM   3735  O  O     . SER J  3 79  ? 29.167  41.245  133.250 1.00 25.16 ? 79   SER B O     1 
ATOM   3736  C  CB    . SER J  3 79  ? 27.660  44.208  133.528 1.00 29.59 ? 79   SER B CB    1 
ATOM   3737  O  OG    . SER J  3 79  ? 26.867  43.324  132.751 1.00 36.38 ? 79   SER B OG    1 
ATOM   3738  N  N     . ALA J  3 80  ? 30.149  42.947  132.138 1.00 21.49 ? 80   ALA B N     1 
ATOM   3739  C  CA    . ALA J  3 80  ? 30.716  42.086  131.113 1.00 23.71 ? 80   ALA B CA    1 
ATOM   3740  C  C     . ALA J  3 80  ? 31.859  41.180  131.611 1.00 24.44 ? 80   ALA B C     1 
ATOM   3741  O  O     . ALA J  3 80  ? 31.924  40.005  131.258 1.00 25.47 ? 80   ALA B O     1 
ATOM   3742  C  CB    . ALA J  3 80  ? 31.200  42.929  129.935 1.00 24.18 ? 80   ALA B CB    1 
ATOM   3743  N  N     . PHE J  3 81  ? 32.757  41.727  132.426 1.00 23.93 ? 81   PHE B N     1 
ATOM   3744  C  CA    . PHE J  3 81  ? 33.899  40.951  132.908 1.00 22.36 ? 81   PHE B CA    1 
ATOM   3745  C  C     . PHE J  3 81  ? 33.445  39.815  133.841 1.00 23.31 ? 81   PHE B C     1 
ATOM   3746  O  O     . PHE J  3 81  ? 34.065  38.759  133.877 1.00 23.18 ? 81   PHE B O     1 
ATOM   3747  C  CB    . PHE J  3 81  ? 34.893  41.878  133.627 1.00 21.02 ? 81   PHE B CB    1 
ATOM   3748  C  CG    . PHE J  3 81  ? 36.191  41.208  134.000 1.00 19.65 ? 81   PHE B CG    1 
ATOM   3749  C  CD1   . PHE J  3 81  ? 37.027  40.684  133.011 1.00 20.57 ? 81   PHE B CD1   1 
ATOM   3750  C  CD2   . PHE J  3 81  ? 36.577  41.114  135.336 1.00 22.34 ? 81   PHE B CD2   1 
ATOM   3751  C  CE1   . PHE J  3 81  ? 38.244  40.065  133.344 1.00 22.13 ? 81   PHE B CE1   1 
ATOM   3752  C  CE2   . PHE J  3 81  ? 37.791  40.497  135.674 1.00 20.30 ? 81   PHE B CE2   1 
ATOM   3753  C  CZ    . PHE J  3 81  ? 38.621  39.977  134.680 1.00 20.79 ? 81   PHE B CZ    1 
ATOM   3754  N  N     . GLU J  3 82  ? 32.359  40.035  134.568 1.00 25.05 ? 82   GLU B N     1 
ATOM   3755  C  CA    . GLU J  3 82  ? 31.829  39.025  135.490 1.00 26.98 ? 82   GLU B CA    1 
ATOM   3756  C  C     . GLU J  3 82  ? 31.494  37.734  134.738 1.00 25.81 ? 82   GLU B C     1 
ATOM   3757  O  O     . GLU J  3 82  ? 31.573  36.643  135.284 1.00 27.21 ? 82   GLU B O     1 
ATOM   3758  C  CB    . GLU J  3 82  ? 30.587  39.590  136.178 1.00 30.35 ? 82   GLU B CB    1 
ATOM   3759  C  CG    . GLU J  3 82  ? 29.806  38.615  137.031 1.00 41.16 ? 82   GLU B CG    1 
ATOM   3760  C  CD    . GLU J  3 82  ? 28.637  39.295  137.725 1.00 48.41 ? 82   GLU B CD    1 
ATOM   3761  O  OE1   . GLU J  3 82  ? 27.910  40.071  137.060 1.00 51.76 ? 82   GLU B OE1   1 
ATOM   3762  O  OE2   . GLU J  3 82  ? 28.441  39.048  138.934 1.00 54.65 ? 82   GLU B OE2   1 
ATOM   3763  N  N     . LYS J  3 83  ? 31.154  37.855  133.469 1.00 25.01 ? 83   LYS B N     1 
ATOM   3764  C  CA    . LYS J  3 83  ? 30.815  36.692  132.666 1.00 25.56 ? 83   LYS B CA    1 
ATOM   3765  C  C     . LYS J  3 83  ? 32.020  35.896  132.167 1.00 24.22 ? 83   LYS B C     1 
ATOM   3766  O  O     . LYS J  3 83  ? 31.858  34.875  131.487 1.00 25.41 ? 83   LYS B O     1 
ATOM   3767  C  CB    . LYS J  3 83  ? 29.966  37.130  131.475 1.00 30.16 ? 83   LYS B CB    1 
ATOM   3768  C  CG    . LYS J  3 83  ? 28.671  37.780  131.912 1.00 30.75 ? 83   LYS B CG    1 
ATOM   3769  C  CD    . LYS J  3 83  ? 27.910  38.394  130.761 1.00 35.14 ? 83   LYS B CD    1 
ATOM   3770  C  CE    . LYS J  3 83  ? 26.629  39.049  131.291 1.00 34.69 ? 83   LYS B CE    1 
ATOM   3771  N  NZ    . LYS J  3 83  ? 25.797  38.065  132.049 1.00 39.06 ? 83   LYS B NZ    1 
ATOM   3772  N  N     . LEU J  3 84  ? 33.228  36.347  132.509 1.00 21.73 ? 84   LEU B N     1 
ATOM   3773  C  CA    . LEU J  3 84  ? 34.434  35.664  132.040 1.00 20.79 ? 84   LEU B CA    1 
ATOM   3774  C  C     . LEU J  3 84  ? 35.182  34.894  133.125 1.00 23.13 ? 84   LEU B C     1 
ATOM   3775  O  O     . LEU J  3 84  ? 36.360  34.564  132.961 1.00 21.80 ? 84   LEU B O     1 
ATOM   3776  C  CB    . LEU J  3 84  ? 35.365  36.689  131.368 1.00 21.15 ? 84   LEU B CB    1 
ATOM   3777  C  CG    . LEU J  3 84  ? 34.800  37.458  130.156 1.00 22.90 ? 84   LEU B CG    1 
ATOM   3778  C  CD1   . LEU J  3 84  ? 35.804  38.543  129.713 1.00 21.06 ? 84   LEU B CD1   1 
ATOM   3779  C  CD2   . LEU J  3 84  ? 34.552  36.488  129.000 1.00 22.24 ? 84   LEU B CD2   1 
ATOM   3780  N  N     . GLN J  3 85  ? 34.492  34.598  134.216 1.00 23.58 ? 85   GLN B N     1 
ATOM   3781  C  CA    . GLN J  3 85  ? 35.088  33.853  135.330 1.00 28.32 ? 85   GLN B CA    1 
ATOM   3782  C  C     . GLN J  3 85  ? 35.742  32.530  134.924 1.00 27.28 ? 85   GLN B C     1 
ATOM   3783  O  O     . GLN J  3 85  ? 36.689  32.094  135.577 1.00 27.39 ? 85   GLN B O     1 
ATOM   3784  C  CB    . GLN J  3 85  ? 34.037  33.579  136.401 1.00 30.94 ? 85   GLN B CB    1 
ATOM   3785  C  CG    . GLN J  3 85  ? 33.612  34.805  137.178 1.00 39.80 ? 85   GLN B CG    1 
ATOM   3786  C  CD    . GLN J  3 85  ? 34.708  35.338  138.074 1.00 42.76 ? 85   GLN B CD    1 
ATOM   3787  O  OE1   . GLN J  3 85  ? 35.278  34.606  138.878 1.00 45.24 ? 85   GLN B OE1   1 
ATOM   3788  N  NE2   . GLN J  3 85  ? 35.000  36.624  137.947 1.00 52.59 ? 85   GLN B NE2   1 
ATOM   3789  N  N     . HIS J  3 86  ? 35.242  31.877  133.869 1.00 27.51 ? 86   HIS B N     1 
ATOM   3790  C  CA    . HIS J  3 86  ? 35.820  30.600  133.417 1.00 26.55 ? 86   HIS B CA    1 
ATOM   3791  C  C     . HIS J  3 86  ? 37.118  30.763  132.616 1.00 28.13 ? 86   HIS B C     1 
ATOM   3792  O  O     . HIS J  3 86  ? 37.838  29.799  132.374 1.00 28.55 ? 86   HIS B O     1 
ATOM   3793  C  CB    . HIS J  3 86  ? 34.807  29.819  132.559 1.00 27.38 ? 86   HIS B CB    1 
ATOM   3794  C  CG    . HIS J  3 86  ? 34.404  30.532  131.310 1.00 22.85 ? 86   HIS B CG    1 
ATOM   3795  N  ND1   . HIS J  3 86  ? 33.676  31.701  131.323 1.00 25.79 ? 86   HIS B ND1   1 
ATOM   3796  C  CD2   . HIS J  3 86  ? 34.652  30.259  130.007 1.00 24.59 ? 86   HIS B CD2   1 
ATOM   3797  C  CE1   . HIS J  3 86  ? 33.492  32.117  130.084 1.00 23.43 ? 86   HIS B CE1   1 
ATOM   3798  N  NE2   . HIS J  3 86  ? 34.076  31.261  129.265 1.00 22.51 ? 86   HIS B NE2   1 
ATOM   3799  N  N     . ILE J  3 87  ? 37.397  31.990  132.192 1.00 24.80 ? 87   ILE B N     1 
ATOM   3800  C  CA    . ILE J  3 87  ? 38.581  32.305  131.422 1.00 23.78 ? 87   ILE B CA    1 
ATOM   3801  C  C     . ILE J  3 87  ? 39.582  33.037  132.330 1.00 20.62 ? 87   ILE B C     1 
ATOM   3802  O  O     . ILE J  3 87  ? 40.786  33.015  132.072 1.00 22.10 ? 87   ILE B O     1 
ATOM   3803  C  CB    . ILE J  3 87  ? 38.211  33.263  130.248 1.00 27.83 ? 87   ILE B CB    1 
ATOM   3804  C  CG1   . ILE J  3 87  ? 37.221  32.570  129.305 1.00 32.25 ? 87   ILE B CG1   1 
ATOM   3805  C  CG2   . ILE J  3 87  ? 39.455  33.693  129.493 1.00 32.14 ? 87   ILE B CG2   1 
ATOM   3806  C  CD1   . ILE J  3 87  ? 37.745  31.301  128.744 1.00 28.79 ? 87   ILE B CD1   1 
ATOM   3807  N  N     . ARG J  3 88  ? 39.057  33.702  133.361 1.00 20.54 ? 88   ARG B N     1 
ATOM   3808  C  CA    . ARG J  3 88  ? 39.875  34.487  134.291 1.00 19.66 ? 88   ARG B CA    1 
ATOM   3809  C  C     . ARG J  3 88  ? 39.200  34.524  135.662 1.00 20.65 ? 88   ARG B C     1 
ATOM   3810  O  O     . ARG J  3 88  ? 38.642  35.527  136.089 1.00 20.95 ? 88   ARG B O     1 
ATOM   3811  C  CB    . ARG J  3 88  ? 40.084  35.907  133.714 1.00 19.46 ? 88   ARG B CB    1 
ATOM   3812  C  CG    . ARG J  3 88  ? 41.229  36.710  134.330 1.00 19.82 ? 88   ARG B CG    1 
ATOM   3813  C  CD    . ARG J  3 88  ? 42.581  36.068  133.997 1.00 21.06 ? 88   ARG B CD    1 
ATOM   3814  N  NE    . ARG J  3 88  ? 43.657  37.046  134.111 1.00 17.97 ? 88   ARG B NE    1 
ATOM   3815  C  CZ    . ARG J  3 88  ? 44.292  37.343  135.236 1.00 19.22 ? 88   ARG B CZ    1 
ATOM   3816  N  NH1   . ARG J  3 88  ? 43.973  36.714  136.369 1.00 17.08 ? 88   ARG B NH1   1 
ATOM   3817  N  NH2   . ARG J  3 88  ? 45.228  38.289  135.223 1.00 19.44 ? 88   ARG B NH2   1 
ATOM   3818  N  N     . PRO J  3 89  ? 39.260  33.398  136.384 1.00 20.46 ? 89   PRO B N     1 
ATOM   3819  C  CA    . PRO J  3 89  ? 38.653  33.275  137.709 1.00 21.70 ? 89   PRO B CA    1 
ATOM   3820  C  C     . PRO J  3 89  ? 39.265  34.173  138.765 1.00 22.40 ? 89   PRO B C     1 
ATOM   3821  O  O     . PRO J  3 89  ? 40.437  34.548  138.683 1.00 23.48 ? 89   PRO B O     1 
ATOM   3822  C  CB    . PRO J  3 89  ? 38.836  31.799  138.033 1.00 22.26 ? 89   PRO B CB    1 
ATOM   3823  C  CG    . PRO J  3 89  ? 40.072  31.455  137.347 1.00 20.85 ? 89   PRO B CG    1 
ATOM   3824  C  CD    . PRO J  3 89  ? 39.989  32.171  136.022 1.00 22.80 ? 89   PRO B CD    1 
ATOM   3825  N  N     . GLY J  3 90  ? 38.446  34.517  139.752 1.00 22.26 ? 90   GLY B N     1 
ATOM   3826  C  CA    . GLY J  3 90  ? 38.898  35.361  140.835 1.00 23.62 ? 90   GLY B CA    1 
ATOM   3827  C  C     . GLY J  3 90  ? 37.770  36.108  141.506 1.00 22.67 ? 90   GLY B C     1 
ATOM   3828  O  O     . GLY J  3 90  ? 36.619  36.058  141.068 1.00 24.34 ? 90   GLY B O     1 
ATOM   3829  N  N     . ASP J  3 91  ? 38.108  36.784  142.596 1.00 18.66 ? 91   ASP B N     1 
ATOM   3830  C  CA    . ASP J  3 91  ? 37.164  37.593  143.345 1.00 20.11 ? 91   ASP B CA    1 
ATOM   3831  C  C     . ASP J  3 91  ? 37.527  39.022  142.902 1.00 22.47 ? 91   ASP B C     1 
ATOM   3832  O  O     . ASP J  3 91  ? 38.406  39.666  143.466 1.00 20.69 ? 91   ASP B O     1 
ATOM   3833  C  CB    . ASP J  3 91  ? 37.403  37.392  144.842 1.00 23.20 ? 91   ASP B CB    1 
ATOM   3834  C  CG    . ASP J  3 91  ? 36.464  38.219  145.702 1.00 26.43 ? 91   ASP B CG    1 
ATOM   3835  O  OD1   . ASP J  3 91  ? 35.534  38.831  145.150 1.00 30.75 ? 91   ASP B OD1   1 
ATOM   3836  O  OD2   . ASP J  3 91  ? 36.657  38.246  146.930 1.00 30.32 ? 91   ASP B OD2   1 
ATOM   3837  N  N     . TRP J  3 92  ? 36.832  39.491  141.880 1.00 20.80 ? 92   TRP B N     1 
ATOM   3838  C  CA    . TRP J  3 92  ? 37.101  40.803  141.291 1.00 21.39 ? 92   TRP B CA    1 
ATOM   3839  C  C     . TRP J  3 92  ? 36.200  41.935  141.747 1.00 23.04 ? 92   TRP B C     1 
ATOM   3840  O  O     . TRP J  3 92  ? 35.007  41.736  142.000 1.00 21.31 ? 92   TRP B O     1 
ATOM   3841  C  CB    . TRP J  3 92  ? 36.978  40.692  139.769 1.00 20.96 ? 92   TRP B CB    1 
ATOM   3842  C  CG    . TRP J  3 92  ? 37.762  39.579  139.152 1.00 21.30 ? 92   TRP B CG    1 
ATOM   3843  C  CD1   . TRP J  3 92  ? 37.303  38.344  138.783 1.00 20.97 ? 92   TRP B CD1   1 
ATOM   3844  C  CD2   . TRP J  3 92  ? 39.149  39.605  138.837 1.00 20.59 ? 92   TRP B CD2   1 
ATOM   3845  N  NE1   . TRP J  3 92  ? 38.331  37.598  138.253 1.00 20.42 ? 92   TRP B NE1   1 
ATOM   3846  C  CE2   . TRP J  3 92  ? 39.477  38.355  138.271 1.00 19.97 ? 92   TRP B CE2   1 
ATOM   3847  C  CE3   . TRP J  3 92  ? 40.158  40.575  138.970 1.00 18.48 ? 92   TRP B CE3   1 
ATOM   3848  C  CZ2   . TRP J  3 92  ? 40.768  38.041  137.843 1.00 19.23 ? 92   TRP B CZ2   1 
ATOM   3849  C  CZ3   . TRP J  3 92  ? 41.439  40.270  138.548 1.00 16.94 ? 92   TRP B CZ3   1 
ATOM   3850  C  CH2   . TRP J  3 92  ? 41.738  39.014  137.985 1.00 18.68 ? 92   TRP B CH2   1 
ATOM   3851  N  N     . ASN J  3 93  ? 36.768  43.131  141.844 1.00 19.99 ? 93   ASN B N     1 
ATOM   3852  C  CA    . ASN J  3 93  ? 35.994  44.312  142.198 1.00 19.81 ? 93   ASN B CA    1 
ATOM   3853  C  C     . ASN J  3 93  ? 36.288  45.379  141.147 1.00 20.56 ? 93   ASN B C     1 
ATOM   3854  O  O     . ASN J  3 93  ? 37.431  45.547  140.736 1.00 19.06 ? 93   ASN B O     1 
ATOM   3855  C  CB    . ASN J  3 93  ? 36.388  44.848  143.570 1.00 26.47 ? 93   ASN B CB    1 
ATOM   3856  C  CG    . ASN J  3 93  ? 35.331  45.782  144.154 1.00 40.09 ? 93   ASN B CG    1 
ATOM   3857  O  OD1   . ASN J  3 93  ? 35.643  46.673  144.960 1.00 46.49 ? 93   ASN B OD1   1 
ATOM   3858  N  ND2   . ASN J  3 93  ? 34.072  45.572  143.767 1.00 41.49 ? 93   ASN B ND2   1 
ATOM   3859  N  N     . VAL J  3 94  ? 35.256  46.092  140.715 1.00 20.90 ? 94   VAL B N     1 
ATOM   3860  C  CA    . VAL J  3 94  ? 35.428  47.159  139.726 1.00 21.73 ? 94   VAL B CA    1 
ATOM   3861  C  C     . VAL J  3 94  ? 34.850  48.400  140.372 1.00 24.88 ? 94   VAL B C     1 
ATOM   3862  O  O     . VAL J  3 94  ? 33.699  48.381  140.815 1.00 25.07 ? 94   VAL B O     1 
ATOM   3863  C  CB    . VAL J  3 94  ? 34.629  46.888  138.430 1.00 20.72 ? 94   VAL B CB    1 
ATOM   3864  C  CG1   . VAL J  3 94  ? 34.782  48.080  137.460 1.00 22.42 ? 94   VAL B CG1   1 
ATOM   3865  C  CG2   . VAL J  3 94  ? 35.108  45.623  137.773 1.00 23.31 ? 94   VAL B CG2   1 
ATOM   3866  N  N     . LYS J  3 95  ? 35.633  49.473  140.466 1.00 21.67 ? 95   LYS B N     1 
ATOM   3867  C  CA    . LYS J  3 95  ? 35.079  50.671  141.056 1.00 25.84 ? 95   LYS B CA    1 
ATOM   3868  C  C     . LYS J  3 95  ? 35.629  51.978  140.550 1.00 26.83 ? 95   LYS B C     1 
ATOM   3869  O  O     . LYS J  3 95  ? 36.814  52.109  140.225 1.00 22.39 ? 95   LYS B O     1 
ATOM   3870  C  CB    . LYS J  3 95  ? 35.196  50.654  142.577 1.00 33.38 ? 95   LYS B CB    1 
ATOM   3871  C  CG    . LYS J  3 95  ? 36.552  50.992  143.133 1.00 34.78 ? 95   LYS B CG    1 
ATOM   3872  C  CD    . LYS J  3 95  ? 36.430  51.174  144.630 1.00 40.76 ? 95   LYS B CD    1 
ATOM   3873  C  CE    . LYS J  3 95  ? 37.712  51.672  145.255 1.00 44.90 ? 95   LYS B CE    1 
ATOM   3874  N  NZ    . LYS J  3 95  ? 37.587  51.704  146.735 1.00 47.64 ? 95   LYS B NZ    1 
ATOM   3875  N  N     . GLN J  3 96  ? 34.728  52.949  140.483 1.00 24.75 ? 96   GLN B N     1 
ATOM   3876  C  CA    . GLN J  3 96  ? 35.089  54.284  140.057 1.00 26.74 ? 96   GLN B CA    1 
ATOM   3877  C  C     . GLN J  3 96  ? 35.750  54.902  141.288 1.00 29.08 ? 96   GLN B C     1 
ATOM   3878  O  O     . GLN J  3 96  ? 35.147  54.958  142.352 1.00 32.51 ? 96   GLN B O     1 
ATOM   3879  C  CB    . GLN J  3 96  ? 33.817  55.029  139.648 1.00 27.05 ? 96   GLN B CB    1 
ATOM   3880  C  CG    . GLN J  3 96  ? 33.942  56.519  139.674 1.00 28.40 ? 96   GLN B CG    1 
ATOM   3881  C  CD    . GLN J  3 96  ? 32.710  57.212  139.144 1.00 27.79 ? 96   GLN B CD    1 
ATOM   3882  O  OE1   . GLN J  3 96  ? 31.594  56.699  139.262 1.00 28.08 ? 96   GLN B OE1   1 
ATOM   3883  N  NE2   . GLN J  3 96  ? 32.901  58.394  138.574 1.00 23.88 ? 96   GLN B NE2   1 
ATOM   3884  N  N     . VAL J  3 97  ? 37.002  55.334  141.159 1.00 30.99 ? 97   VAL B N     1 
ATOM   3885  C  CA    . VAL J  3 97  ? 37.711  55.927  142.290 1.00 39.63 ? 97   VAL B CA    1 
ATOM   3886  C  C     . VAL J  3 97  ? 37.538  57.423  142.216 1.00 47.35 ? 97   VAL B C     1 
ATOM   3887  O  O     . VAL J  3 97  ? 37.889  58.037  141.216 1.00 50.32 ? 97   VAL B O     1 
ATOM   3888  C  CB    . VAL J  3 97  ? 39.232  55.679  142.243 1.00 40.98 ? 97   VAL B CB    1 
ATOM   3889  C  CG1   . VAL J  3 97  ? 39.863  56.121  143.566 1.00 42.97 ? 97   VAL B CG1   1 
ATOM   3890  C  CG2   . VAL J  3 97  ? 39.529  54.226  141.931 1.00 43.54 ? 97   VAL B CG2   1 
ATOM   3891  N  N     . GLY J  3 98  ? 37.025  58.031  143.268 1.00 51.44 ? 98   GLY B N     1 
ATOM   3892  C  CA    . GLY J  3 98  ? 36.858  59.461  143.194 1.00 54.24 ? 98   GLY B CA    1 
ATOM   3893  C  C     . GLY J  3 98  ? 38.179  60.201  143.233 1.00 56.59 ? 98   GLY B C     1 
ATOM   3894  O  O     . GLY J  3 98  ? 39.130  59.764  143.894 1.00 58.44 ? 98   GLY B O     1 
ATOM   3895  N  N     . SER J  3 99  ? 38.258  61.318  142.513 1.00 57.24 ? 99   SER B N     1 
ATOM   3896  C  CA    . SER J  3 99  ? 39.466  62.132  142.551 1.00 59.34 ? 99   SER B CA    1 
ATOM   3897  C  C     . SER J  3 99  ? 39.539  62.432  144.051 1.00 60.04 ? 99   SER B C     1 
ATOM   3898  O  O     . SER J  3 99  ? 40.519  62.967  144.572 1.00 60.04 ? 99   SER B O     1 
ATOM   3899  C  CB    . SER J  3 99  ? 39.264  63.423  141.755 1.00 59.60 ? 99   SER B CB    1 
ATOM   3900  O  OG    . SER J  3 99  ? 38.303  64.262  142.374 1.00 60.04 ? 99   SER B OG    1 
ATOM   3901  N  N     . ARG J  3 100 ? 38.443  62.063  144.710 1.00 60.04 ? 100  ARG B N     1 
ATOM   3902  C  CA    . ARG J  3 100 ? 38.225  62.188  146.141 1.00 60.01 ? 100  ARG B CA    1 
ATOM   3903  C  C     . ARG J  3 100 ? 38.930  61.036  146.864 1.00 60.04 ? 100  ARG B C     1 
ATOM   3904  O  O     . ARG J  3 100 ? 38.429  60.528  147.876 1.00 60.04 ? 100  ARG B O     1 
ATOM   3905  C  CB    . ARG J  3 100 ? 36.715  62.127  146.431 1.00 60.04 ? 100  ARG B CB    1 
ATOM   3906  C  CG    . ARG J  3 100 ? 35.850  61.672  145.238 1.00 60.04 ? 100  ARG B CG    1 
ATOM   3907  C  CD    . ARG J  3 100 ? 34.994  60.424  145.528 1.00 60.04 ? 100  ARG B CD    1 
ATOM   3908  N  NE    . ARG J  3 100 ? 34.193  60.043  144.358 1.00 60.04 ? 100  ARG B NE    1 
ATOM   3909  C  CZ    . ARG J  3 100 ? 33.581  58.867  144.199 1.00 60.04 ? 100  ARG B CZ    1 
ATOM   3910  N  NH1   . ARG J  3 100 ? 33.668  57.932  145.140 1.00 60.04 ? 100  ARG B NH1   1 
ATOM   3911  N  NH2   . ARG J  3 100 ? 32.890  58.620  143.088 1.00 60.04 ? 100  ARG B NH2   1 
ATOM   3912  N  N     . ASN J  3 101 ? 40.087  60.615  146.352 1.00 58.45 ? 101  ASN B N     1 
ATOM   3913  C  CA    . ASN J  3 101 ? 40.804  59.525  146.995 1.00 55.85 ? 101  ASN B CA    1 
ATOM   3914  C  C     . ASN J  3 101 ? 42.265  59.343  146.564 1.00 54.00 ? 101  ASN B C     1 
ATOM   3915  O  O     . ASN J  3 101 ? 42.577  58.522  145.697 1.00 53.11 ? 101  ASN B O     1 
ATOM   3916  C  CB    . ASN J  3 101 ? 40.037  58.219  146.780 1.00 56.68 ? 101  ASN B CB    1 
ATOM   3917  C  CG    . ASN J  3 101 ? 40.371  57.173  147.820 1.00 58.85 ? 101  ASN B CG    1 
ATOM   3918  O  OD1   . ASN J  3 101 ? 41.530  57.019  148.219 1.00 60.04 ? 101  ASN B OD1   1 
ATOM   3919  N  ND2   . ASN J  3 101 ? 39.358  56.434  148.258 1.00 60.04 ? 101  ASN B ND2   1 
ATOM   3920  N  N     . ARG J  3 102 ? 43.162  60.109  147.179 1.00 52.73 ? 102  ARG B N     1 
ATOM   3921  C  CA    . ARG J  3 102 ? 44.587  60.002  146.884 1.00 49.58 ? 102  ARG B CA    1 
ATOM   3922  C  C     . ARG J  3 102 ? 45.114  58.818  147.701 1.00 48.17 ? 102  ARG B C     1 
ATOM   3923  O  O     . ARG J  3 102 ? 44.628  58.542  148.804 1.00 46.74 ? 102  ARG B O     1 
ATOM   3924  C  CB    . ARG J  3 102 ? 45.334  61.277  147.299 1.00 52.07 ? 102  ARG B CB    1 
ATOM   3925  C  CG    . ARG J  3 102 ? 44.889  62.573  146.620 1.00 55.31 ? 102  ARG B CG    1 
ATOM   3926  C  CD    . ARG J  3 102 ? 45.719  63.750  147.153 1.00 57.98 ? 102  ARG B CD    1 
ATOM   3927  N  NE    . ARG J  3 102 ? 45.013  65.032  147.098 1.00 60.04 ? 102  ARG B NE    1 
ATOM   3928  C  CZ    . ARG J  3 102 ? 45.363  66.107  147.806 1.00 60.04 ? 102  ARG B CZ    1 
ATOM   3929  N  NH1   . ARG J  3 102 ? 46.410  66.057  148.624 1.00 60.04 ? 102  ARG B NH1   1 
ATOM   3930  N  NH2   . ARG J  3 102 ? 44.663  67.234  147.708 1.00 60.04 ? 102  ARG B NH2   1 
ATOM   3931  N  N     . LEU J  3 103 ? 46.110  58.122  147.169 1.00 45.25 ? 103  LEU B N     1 
ATOM   3932  C  CA    . LEU J  3 103 ? 46.675  56.958  147.851 1.00 45.50 ? 103  LEU B CA    1 
ATOM   3933  C  C     . LEU J  3 103 ? 45.714  55.765  147.989 1.00 43.07 ? 103  LEU B C     1 
ATOM   3934  O  O     . LEU J  3 103 ? 45.979  54.838  148.761 1.00 42.03 ? 103  LEU B O     1 
ATOM   3935  C  CB    . LEU J  3 103 ? 47.228  57.337  149.237 1.00 47.06 ? 103  LEU B CB    1 
ATOM   3936  C  CG    . LEU J  3 103 ? 48.625  57.980  149.298 1.00 50.66 ? 103  LEU B CG    1 
ATOM   3937  C  CD1   . LEU J  3 103 ? 49.076  58.103  150.748 1.00 51.08 ? 103  LEU B CD1   1 
ATOM   3938  C  CD2   . LEU J  3 103 ? 49.629  57.133  148.522 1.00 51.74 ? 103  LEU B CD2   1 
ATOM   3939  N  N     . GLU J  3 104 ? 44.588  55.787  147.275 1.00 38.14 ? 104  GLU B N     1 
ATOM   3940  C  CA    . GLU J  3 104 ? 43.693  54.632  147.306 1.00 33.17 ? 104  GLU B CA    1 
ATOM   3941  C  C     . GLU J  3 104 ? 44.562  53.551  146.660 1.00 30.82 ? 104  GLU B C     1 
ATOM   3942  O  O     . GLU J  3 104 ? 44.509  52.376  147.014 1.00 30.55 ? 104  GLU B O     1 
ATOM   3943  C  CB    . GLU J  3 104 ? 42.432  54.903  146.466 1.00 35.75 ? 104  GLU B CB    1 
ATOM   3944  C  CG    . GLU J  3 104 ? 41.702  53.677  145.871 1.00 35.45 ? 104  GLU B CG    1 
ATOM   3945  C  CD    . GLU J  3 104 ? 40.909  52.871  146.880 1.00 43.52 ? 104  GLU B CD    1 
ATOM   3946  O  OE1   . GLU J  3 104 ? 40.543  53.429  147.946 1.00 44.78 ? 104  GLU B OE1   1 
ATOM   3947  O  OE2   . GLU J  3 104 ? 40.634  51.674  146.602 1.00 39.30 ? 104  GLU B OE2   1 
ATOM   3948  N  N     . ILE J  3 105 ? 45.401  53.990  145.734 1.00 29.05 ? 105  ILE B N     1 
ATOM   3949  C  CA    . ILE J  3 105 ? 46.290  53.096  145.017 1.00 27.80 ? 105  ILE B CA    1 
ATOM   3950  C  C     . ILE J  3 105 ? 47.235  52.319  145.933 1.00 26.35 ? 105  ILE B C     1 
ATOM   3951  O  O     . ILE J  3 105 ? 47.605  51.176  145.631 1.00 24.30 ? 105  ILE B O     1 
ATOM   3952  C  CB    . ILE J  3 105 ? 47.098  53.885  143.963 1.00 33.18 ? 105  ILE B CB    1 
ATOM   3953  C  CG1   . ILE J  3 105 ? 47.900  52.917  143.116 1.00 32.42 ? 105  ILE B CG1   1 
ATOM   3954  C  CG2   . ILE J  3 105 ? 48.023  54.892  144.636 1.00 34.43 ? 105  ILE B CG2   1 
ATOM   3955  C  CD1   . ILE J  3 105 ? 47.728  53.149  141.652 1.00 39.10 ? 105  ILE B CD1   1 
ATOM   3956  N  N     . ALA J  3 106 ? 47.602  52.922  147.066 1.00 23.95 ? 106  ALA B N     1 
ATOM   3957  C  CA    . ALA J  3 106 ? 48.500  52.274  148.021 1.00 23.33 ? 106  ALA B CA    1 
ATOM   3958  C  C     . ALA J  3 106 ? 47.786  51.203  148.843 1.00 24.77 ? 106  ALA B C     1 
ATOM   3959  O  O     . ALA J  3 106 ? 48.402  50.521  149.670 1.00 24.03 ? 106  ALA B O     1 
ATOM   3960  C  CB    . ALA J  3 106 ? 49.135  53.318  148.928 1.00 23.09 ? 106  ALA B CB    1 
ATOM   3961  N  N     . ARG J  3 107 ? 46.483  51.055  148.620 1.00 23.38 ? 107  ARG B N     1 
ATOM   3962  C  CA    . ARG J  3 107 ? 45.745  50.006  149.304 1.00 24.96 ? 107  ARG B CA    1 
ATOM   3963  C  C     . ARG J  3 107 ? 46.059  48.680  148.606 1.00 24.73 ? 107  ARG B C     1 
ATOM   3964  O  O     . ARG J  3 107 ? 45.777  47.610  149.146 1.00 26.58 ? 107  ARG B O     1 
ATOM   3965  C  CB    . ARG J  3 107 ? 44.235  50.249  149.226 1.00 28.38 ? 107  ARG B CB    1 
ATOM   3966  C  CG    . ARG J  3 107 ? 43.765  51.572  149.819 1.00 36.32 ? 107  ARG B CG    1 
ATOM   3967  C  CD    . ARG J  3 107 ? 42.233  51.664  149.785 1.00 42.28 ? 107  ARG B CD    1 
ATOM   3968  N  NE    . ARG J  3 107 ? 41.635  51.459  151.100 1.00 51.45 ? 107  ARG B NE    1 
ATOM   3969  C  CZ    . ARG J  3 107 ? 40.413  50.971  151.309 1.00 54.72 ? 107  ARG B CZ    1 
ATOM   3970  N  NH1   . ARG J  3 107 ? 39.639  50.622  150.287 1.00 56.52 ? 107  ARG B NH1   1 
ATOM   3971  N  NH2   . ARG J  3 107 ? 39.959  50.838  152.551 1.00 58.51 ? 107  ARG B NH2   1 
ATOM   3972  N  N     . TYR J  3 108 ? 46.646  48.749  147.404 1.00 22.32 ? 108  TYR B N     1 
ATOM   3973  C  CA    . TYR J  3 108 ? 46.947  47.540  146.642 1.00 20.95 ? 108  TYR B CA    1 
ATOM   3974  C  C     . TYR J  3 108 ? 48.395  47.121  146.702 1.00 20.59 ? 108  TYR B C     1 
ATOM   3975  O  O     . TYR J  3 108 ? 49.291  47.950  146.803 1.00 19.03 ? 108  TYR B O     1 
ATOM   3976  C  CB    . TYR J  3 108 ? 46.438  47.705  145.202 1.00 21.73 ? 108  TYR B CB    1 
ATOM   3977  C  CG    . TYR J  3 108 ? 44.986  48.093  145.262 1.00 21.85 ? 108  TYR B CG    1 
ATOM   3978  C  CD1   . TYR J  3 108 ? 44.592  49.417  145.100 1.00 22.03 ? 108  TYR B CD1   1 
ATOM   3979  C  CD2   . TYR J  3 108 ? 44.025  47.160  145.664 1.00 24.85 ? 108  TYR B CD2   1 
ATOM   3980  C  CE1   . TYR J  3 108 ? 43.277  49.810  145.353 1.00 24.61 ? 108  TYR B CE1   1 
ATOM   3981  C  CE2   . TYR J  3 108 ? 42.715  47.535  145.923 1.00 28.89 ? 108  TYR B CE2   1 
ATOM   3982  C  CZ    . TYR J  3 108 ? 42.347  48.856  145.771 1.00 25.10 ? 108  TYR B CZ    1 
ATOM   3983  O  OH    . TYR J  3 108 ? 41.053  49.217  146.073 1.00 31.43 ? 108  TYR B OH    1 
ATOM   3984  N  N     . GLN J  3 109 ? 48.596  45.812  146.654 1.00 21.00 ? 109  GLN B N     1 
ATOM   3985  C  CA    . GLN J  3 109 ? 49.894  45.205  146.814 1.00 20.75 ? 109  GLN B CA    1 
ATOM   3986  C  C     . GLN J  3 109 ? 51.067  45.802  146.035 1.00 18.53 ? 109  GLN B C     1 
ATOM   3987  O  O     . GLN J  3 109 ? 52.118  46.119  146.618 1.00 21.14 ? 109  GLN B O     1 
ATOM   3988  C  CB    . GLN J  3 109 ? 49.771  43.716  146.501 1.00 23.43 ? 109  GLN B CB    1 
ATOM   3989  C  CG    . GLN J  3 109 ? 50.906  42.889  147.039 1.00 28.42 ? 109  GLN B CG    1 
ATOM   3990  C  CD    . GLN J  3 109 ? 50.729  41.409  146.720 1.00 33.60 ? 109  GLN B CD    1 
ATOM   3991  O  OE1   . GLN J  3 109 ? 51.660  40.757  146.273 1.00 35.74 ? 109  GLN B OE1   1 
ATOM   3992  N  NE2   . GLN J  3 109 ? 49.526  40.883  146.941 1.00 36.78 ? 109  GLN B NE2   1 
ATOM   3993  N  N     . GLN J  3 110 ? 50.896  45.993  144.737 1.00 16.63 ? 110  GLN B N     1 
ATOM   3994  C  CA    . GLN J  3 110 ? 52.020  46.506  143.963 1.00 19.04 ? 110  GLN B CA    1 
ATOM   3995  C  C     . GLN J  3 110 ? 52.466  47.919  144.287 1.00 16.95 ? 110  GLN B C     1 
ATOM   3996  O  O     . GLN J  3 110 ? 53.560  48.313  143.896 1.00 16.93 ? 110  GLN B O     1 
ATOM   3997  C  CB    . GLN J  3 110 ? 51.742  46.438  142.448 1.00 17.89 ? 110  GLN B CB    1 
ATOM   3998  C  CG    . GLN J  3 110 ? 51.263  45.073  141.927 1.00 17.95 ? 110  GLN B CG    1 
ATOM   3999  C  CD    . GLN J  3 110 ? 49.770  45.088  141.686 1.00 20.83 ? 110  GLN B CD    1 
ATOM   4000  O  OE1   . GLN J  3 110 ? 48.983  45.240  142.631 1.00 19.20 ? 110  GLN B OE1   1 
ATOM   4001  N  NE2   . GLN J  3 110 ? 49.368  44.982  140.413 1.00 24.11 ? 110  GLN B NE2   1 
ATOM   4002  N  N     . TYR J  3 111 ? 51.629  48.690  144.988 1.00 17.18 ? 111  TYR B N     1 
ATOM   4003  C  CA    . TYR J  3 111 ? 51.962  50.082  145.299 1.00 15.21 ? 111  TYR B CA    1 
ATOM   4004  C  C     . TYR J  3 111 ? 51.849  50.428  146.785 1.00 15.99 ? 111  TYR B C     1 
ATOM   4005  O  O     . TYR J  3 111 ? 51.887  51.605  147.150 1.00 18.55 ? 111  TYR B O     1 
ATOM   4006  C  CB    . TYR J  3 111 ? 51.039  51.010  144.479 1.00 18.47 ? 111  TYR B CB    1 
ATOM   4007  C  CG    . TYR J  3 111 ? 51.159  50.756  142.995 1.00 16.20 ? 111  TYR B CG    1 
ATOM   4008  C  CD1   . TYR J  3 111 ? 50.271  49.901  142.326 1.00 17.40 ? 111  TYR B CD1   1 
ATOM   4009  C  CD2   . TYR J  3 111 ? 52.223  51.301  142.279 1.00 15.18 ? 111  TYR B CD2   1 
ATOM   4010  C  CE1   . TYR J  3 111 ? 50.464  49.593  140.960 1.00 16.57 ? 111  TYR B CE1   1 
ATOM   4011  C  CE2   . TYR J  3 111 ? 52.420  51.005  140.918 1.00 16.64 ? 111  TYR B CE2   1 
ATOM   4012  C  CZ    . TYR J  3 111 ? 51.542  50.153  140.275 1.00 16.28 ? 111  TYR B CZ    1 
ATOM   4013  O  OH    . TYR J  3 111 ? 51.754  49.829  138.938 1.00 15.28 ? 111  TYR B OH    1 
ATOM   4014  N  N     . ALA J  3 112 ? 51.780  49.402  147.627 1.00 19.22 ? 112  ALA B N     1 
ATOM   4015  C  CA    . ALA J  3 112 ? 51.614  49.606  149.072 1.00 20.55 ? 112  ALA B CA    1 
ATOM   4016  C  C     . ALA J  3 112 ? 52.715  50.456  149.692 1.00 22.39 ? 112  ALA B C     1 
ATOM   4017  O  O     . ALA J  3 112 ? 52.475  51.225  150.649 1.00 21.30 ? 112  ALA B O     1 
ATOM   4018  C  CB    . ALA J  3 112 ? 51.534  48.249  149.777 1.00 22.45 ? 112  ALA B CB    1 
ATOM   4019  N  N     . HIS J  3 113 ? 53.920  50.327  149.149 1.00 19.79 ? 113  HIS B N     1 
ATOM   4020  C  CA    . HIS J  3 113 ? 55.063  51.087  149.648 1.00 19.13 ? 113  HIS B CA    1 
ATOM   4021  C  C     . HIS J  3 113 ? 54.934  52.585  149.464 1.00 19.67 ? 113  HIS B C     1 
ATOM   4022  O  O     . HIS J  3 113 ? 55.697  53.346  150.066 1.00 24.07 ? 113  HIS B O     1 
ATOM   4023  C  CB    . HIS J  3 113 ? 56.361  50.603  148.988 1.00 19.55 ? 113  HIS B CB    1 
ATOM   4024  C  CG    . HIS J  3 113 ? 56.336  50.672  147.492 1.00 16.86 ? 113  HIS B CG    1 
ATOM   4025  N  ND1   . HIS J  3 113 ? 55.544  49.848  146.723 1.00 16.90 ? 113  HIS B ND1   1 
ATOM   4026  C  CD2   . HIS J  3 113 ? 56.994  51.484  146.632 1.00 19.13 ? 113  HIS B CD2   1 
ATOM   4027  C  CE1   . HIS J  3 113 ? 55.718  50.150  145.444 1.00 15.23 ? 113  HIS B CE1   1 
ATOM   4028  N  NE2   . HIS J  3 113 ? 56.591  51.138  145.360 1.00 16.87 ? 113  HIS B NE2   1 
ATOM   4029  N  N     . LEU J  3 114 ? 53.979  53.033  148.640 1.00 20.83 ? 114  LEU B N     1 
ATOM   4030  C  CA    . LEU J  3 114 ? 53.828  54.462  148.441 1.00 23.32 ? 114  LEU B CA    1 
ATOM   4031  C  C     . LEU J  3 114 ? 53.399  55.163  149.734 1.00 23.73 ? 114  LEU B C     1 
ATOM   4032  O  O     . LEU J  3 114 ? 53.655  56.350  149.913 1.00 27.14 ? 114  LEU B O     1 
ATOM   4033  C  CB    . LEU J  3 114 ? 52.838  54.762  147.307 1.00 23.07 ? 114  LEU B CB    1 
ATOM   4034  C  CG    . LEU J  3 114 ? 53.280  54.275  145.921 1.00 25.92 ? 114  LEU B CG    1 
ATOM   4035  C  CD1   . LEU J  3 114 ? 52.295  54.837  144.882 1.00 27.75 ? 114  LEU B CD1   1 
ATOM   4036  C  CD2   . LEU J  3 114 ? 54.695  54.725  145.599 1.00 30.03 ? 114  LEU B CD2   1 
ATOM   4037  N  N     . THR J  3 115 ? 52.766  54.423  150.644 1.00 25.28 ? 115  THR B N     1 
ATOM   4038  C  CA    . THR J  3 115 ? 52.345  55.014  151.920 1.00 28.08 ? 115  THR B CA    1 
ATOM   4039  C  C     . THR J  3 115 ? 53.587  55.349  152.736 1.00 28.44 ? 115  THR B C     1 
ATOM   4040  O  O     . THR J  3 115 ? 53.670  56.404  153.355 1.00 29.97 ? 115  THR B O     1 
ATOM   4041  C  CB    . THR J  3 115 ? 51.479  54.040  152.739 1.00 27.76 ? 115  THR B CB    1 
ATOM   4042  O  OG1   . THR J  3 115 ? 50.298  53.730  151.999 1.00 26.90 ? 115  THR B OG1   1 
ATOM   4043  C  CG2   . THR J  3 115 ? 51.077  54.667  154.088 1.00 29.04 ? 115  THR B CG2   1 
ATOM   4044  N  N     . ALA J  3 116 ? 54.559  54.443  152.726 1.00 26.93 ? 116  ALA B N     1 
ATOM   4045  C  CA    . ALA J  3 116 ? 55.785  54.666  153.479 1.00 31.51 ? 116  ALA B CA    1 
ATOM   4046  C  C     . ALA J  3 116 ? 56.564  55.831  152.862 1.00 31.22 ? 116  ALA B C     1 
ATOM   4047  O  O     . ALA J  3 116 ? 57.230  56.585  153.569 1.00 31.80 ? 116  ALA B O     1 
ATOM   4048  C  CB    . ALA J  3 116 ? 56.632  53.397  153.489 1.00 32.73 ? 116  ALA B CB    1 
ATOM   4049  N  N     . LEU J  3 117 ? 56.484  55.990  151.546 1.00 29.95 ? 117  LEU B N     1 
ATOM   4050  C  CA    . LEU J  3 117 ? 57.185  57.092  150.898 1.00 28.88 ? 117  LEU B CA    1 
ATOM   4051  C  C     . LEU J  3 117 ? 56.522  58.406  151.300 1.00 29.59 ? 117  LEU B C     1 
ATOM   4052  O  O     . LEU J  3 117 ? 57.197  59.404  151.563 1.00 29.62 ? 117  LEU B O     1 
ATOM   4053  C  CB    . LEU J  3 117 ? 57.148  56.953  149.375 1.00 28.77 ? 117  LEU B CB    1 
ATOM   4054  C  CG    . LEU J  3 117 ? 58.065  55.900  148.763 1.00 32.76 ? 117  LEU B CG    1 
ATOM   4055  C  CD1   . LEU J  3 117 ? 57.975  55.925  147.228 1.00 35.10 ? 117  LEU B CD1   1 
ATOM   4056  C  CD2   . LEU J  3 117 ? 59.475  56.180  149.203 1.00 39.44 ? 117  LEU B CD2   1 
ATOM   4057  N  N     . ALA J  3 118 ? 55.197  58.397  151.349 1.00 28.41 ? 118  ALA B N     1 
ATOM   4058  C  CA    . ALA J  3 118 ? 54.454  59.584  151.718 1.00 30.84 ? 118  ALA B CA    1 
ATOM   4059  C  C     . ALA J  3 118 ? 54.737  59.961  153.168 1.00 34.83 ? 118  ALA B C     1 
ATOM   4060  O  O     . ALA J  3 118 ? 54.912  61.135  153.475 1.00 35.04 ? 118  ALA B O     1 
ATOM   4061  C  CB    . ALA J  3 118 ? 52.962  59.363  151.498 1.00 30.95 ? 118  ALA B CB    1 
ATOM   4062  N  N     . LYS J  3 119 ? 54.803  58.983  154.066 1.00 36.16 ? 119  LYS B N     1 
ATOM   4063  C  CA    . LYS J  3 119 ? 55.080  59.316  155.467 1.00 39.94 ? 119  LYS B CA    1 
ATOM   4064  C  C     . LYS J  3 119 ? 56.502  59.825  155.648 1.00 41.63 ? 119  LYS B C     1 
ATOM   4065  O  O     . LYS J  3 119 ? 56.757  60.730  156.442 1.00 43.17 ? 119  LYS B O     1 
ATOM   4066  C  CB    . LYS J  3 119 ? 54.847  58.111  156.365 1.00 43.41 ? 119  LYS B CB    1 
ATOM   4067  C  CG    . LYS J  3 119 ? 53.401  57.666  156.397 1.00 48.20 ? 119  LYS B CG    1 
ATOM   4068  C  CD    . LYS J  3 119 ? 53.189  56.635  157.491 1.00 52.77 ? 119  LYS B CD    1 
ATOM   4069  C  CE    . LYS J  3 119 ? 51.824  55.978  157.389 1.00 54.52 ? 119  LYS B CE    1 
ATOM   4070  N  NZ    . LYS J  3 119 ? 51.735  54.814  158.312 1.00 58.42 ? 119  LYS B NZ    1 
ATOM   4071  N  N     . ALA J  3 120 ? 57.433  59.242  154.907 1.00 41.69 ? 120  ALA B N     1 
ATOM   4072  C  CA    . ALA J  3 120 ? 58.819  59.667  154.983 1.00 42.16 ? 120  ALA B CA    1 
ATOM   4073  C  C     . ALA J  3 120 ? 58.906  61.129  154.528 1.00 43.08 ? 120  ALA B C     1 
ATOM   4074  O  O     . ALA J  3 120 ? 59.651  61.928  155.096 1.00 42.21 ? 120  ALA B O     1 
ATOM   4075  C  CB    . ALA J  3 120 ? 59.684  58.791  154.084 1.00 42.56 ? 120  ALA B CB    1 
ATOM   4076  N  N     . ALA J  3 121 ? 58.143  61.473  153.497 1.00 40.66 ? 121  ALA B N     1 
ATOM   4077  C  CA    . ALA J  3 121 ? 58.156  62.836  152.976 1.00 43.77 ? 121  ALA B CA    1 
ATOM   4078  C  C     . ALA J  3 121 ? 57.509  63.806  153.951 1.00 45.20 ? 121  ALA B C     1 
ATOM   4079  O  O     . ALA J  3 121 ? 57.914  64.964  154.047 1.00 42.25 ? 121  ALA B O     1 
ATOM   4080  C  CB    . ALA J  3 121 ? 57.439  62.895  151.628 1.00 41.18 ? 121  ALA B CB    1 
ATOM   4081  N  N     . GLU J  3 122 ? 56.502  63.340  154.678 1.00 48.06 ? 122  GLU B N     1 
ATOM   4082  C  CA    . GLU J  3 122 ? 55.826  64.207  155.632 1.00 51.95 ? 122  GLU B CA    1 
ATOM   4083  C  C     . GLU J  3 122 ? 56.718  64.646  156.785 1.00 53.18 ? 122  GLU B C     1 
ATOM   4084  O  O     . GLU J  3 122 ? 56.453  65.662  157.429 1.00 55.62 ? 122  GLU B O     1 
ATOM   4085  C  CB    . GLU J  3 122 ? 54.587  63.520  156.192 1.00 54.33 ? 122  GLU B CB    1 
ATOM   4086  C  CG    . GLU J  3 122 ? 54.087  64.167  157.466 1.00 57.35 ? 122  GLU B CG    1 
ATOM   4087  C  CD    . GLU J  3 122 ? 52.759  63.622  157.909 1.00 60.04 ? 122  GLU B CD    1 
ATOM   4088  O  OE1   . GLU J  3 122 ? 52.638  62.381  158.035 1.00 60.04 ? 122  GLU B OE1   1 
ATOM   4089  O  OE2   . GLU J  3 122 ? 51.835  64.436  158.133 1.00 60.04 ? 122  GLU B OE2   1 
ATOM   4090  N  N     . GLU J  3 123 ? 57.769  63.885  157.055 1.00 54.11 ? 123  GLU B N     1 
ATOM   4091  C  CA    . GLU J  3 123 ? 58.672  64.229  158.144 1.00 55.69 ? 123  GLU B CA    1 
ATOM   4092  C  C     . GLU J  3 123 ? 60.015  64.678  157.587 1.00 54.61 ? 123  GLU B C     1 
ATOM   4093  O  O     . GLU J  3 123 ? 60.857  65.222  158.296 1.00 54.50 ? 123  GLU B O     1 
ATOM   4094  C  CB    . GLU J  3 123 ? 58.853  63.024  159.072 1.00 57.60 ? 123  GLU B CB    1 
ATOM   4095  C  CG    . GLU J  3 123 ? 59.724  61.913  158.513 1.00 58.60 ? 123  GLU B CG    1 
ATOM   4096  C  CD    . GLU J  3 123 ? 59.608  60.635  159.321 1.00 60.04 ? 123  GLU B CD    1 
ATOM   4097  O  OE1   . GLU J  3 123 ? 58.594  59.923  159.157 1.00 60.04 ? 123  GLU B OE1   1 
ATOM   4098  O  OE2   . GLU J  3 123 ? 60.520  60.346  160.129 1.00 60.04 ? 123  GLU B OE2   1 
ATOM   4099  N  N     . ASN J  3 124 ? 60.199  64.451  156.295 1.00 56.25 ? 124  ASN B N     1 
ATOM   4100  C  CA    . ASN J  3 124 ? 61.426  64.833  155.637 1.00 55.00 ? 124  ASN B CA    1 
ATOM   4101  C  C     . ASN J  3 124 ? 61.105  65.822  154.537 1.00 56.48 ? 124  ASN B C     1 
ATOM   4102  O  O     . ASN J  3 124 ? 61.309  65.542  153.340 1.00 53.32 ? 124  ASN B O     1 
ATOM   4103  C  CB    . ASN J  3 124 ? 62.123  63.594  155.074 1.00 57.33 ? 124  ASN B CB    1 
ATOM   4104  C  CG    . ASN J  3 124 ? 62.514  62.602  156.167 1.00 60.03 ? 124  ASN B CG    1 
ATOM   4105  O  OD1   . ASN J  3 124 ? 62.308  61.390  156.029 1.00 60.04 ? 124  ASN B OD1   1 
ATOM   4106  N  ND2   . ASN J  3 124 ? 63.088  63.116  157.260 1.00 60.02 ? 124  ASN B ND2   1 
ATOM   4107  N  N     . PRO J  3 125 ? 60.552  66.989  154.924 1.00 57.16 ? 125  PRO B N     1 
ATOM   4108  C  CA    . PRO J  3 125 ? 60.228  67.996  153.916 1.00 58.99 ? 125  PRO B CA    1 
ATOM   4109  C  C     . PRO J  3 125 ? 61.497  68.087  153.099 1.00 57.78 ? 125  PRO B C     1 
ATOM   4110  O  O     . PRO J  3 125 ? 62.590  68.001  153.667 1.00 59.37 ? 125  PRO B O     1 
ATOM   4111  C  CB    . PRO J  3 125 ? 59.985  69.246  154.749 1.00 59.86 ? 125  PRO B CB    1 
ATOM   4112  C  CG    . PRO J  3 125 ? 59.348  68.683  155.986 1.00 57.95 ? 125  PRO B CG    1 
ATOM   4113  C  CD    . PRO J  3 125 ? 60.235  67.484  156.277 1.00 57.33 ? 125  PRO B CD    1 
ATOM   4114  N  N     . GLU J  3 126 ? 61.346  68.223  151.785 1.00 56.85 ? 126  GLU B N     1 
ATOM   4115  C  CA    . GLU J  3 126 ? 62.471  68.296  150.862 1.00 56.17 ? 126  GLU B CA    1 
ATOM   4116  C  C     . GLU J  3 126 ? 62.444  67.044  150.008 1.00 54.74 ? 126  GLU B C     1 
ATOM   4117  O  O     . GLU J  3 126 ? 62.578  67.120  148.783 1.00 54.56 ? 126  GLU B O     1 
ATOM   4118  C  CB    . GLU J  3 126 ? 63.811  68.380  151.617 1.00 58.71 ? 126  GLU B CB    1 
ATOM   4119  C  CG    . GLU J  3 126 ? 65.061  68.328  150.748 1.00 60.03 ? 126  GLU B CG    1 
ATOM   4120  C  CD    . GLU J  3 126 ? 66.350  68.280  151.569 1.00 60.03 ? 126  GLU B CD    1 
ATOM   4121  O  OE1   . GLU J  3 126 ? 66.272  68.099  152.804 1.00 60.02 ? 126  GLU B OE1   1 
ATOM   4122  O  OE2   . GLU J  3 126 ? 67.447  68.414  150.980 1.00 60.04 ? 126  GLU B OE2   1 
ATOM   4123  N  N     . LEU J  3 127 ? 62.277  65.893  150.662 1.00 51.36 ? 127  LEU B N     1 
ATOM   4124  C  CA    . LEU J  3 127 ? 62.223  64.619  149.953 1.00 46.12 ? 127  LEU B CA    1 
ATOM   4125  C  C     . LEU J  3 127 ? 61.104  64.680  148.926 1.00 45.01 ? 127  LEU B C     1 
ATOM   4126  O  O     . LEU J  3 127 ? 61.190  64.058  147.867 1.00 42.69 ? 127  LEU B O     1 
ATOM   4127  C  CB    . LEU J  3 127 ? 61.941  63.461  150.911 1.00 46.03 ? 127  LEU B CB    1 
ATOM   4128  C  CG    . LEU J  3 127 ? 63.035  62.968  151.863 1.00 49.50 ? 127  LEU B CG    1 
ATOM   4129  C  CD1   . LEU J  3 127 ? 62.563  61.688  152.554 1.00 45.27 ? 127  LEU B CD1   1 
ATOM   4130  C  CD2   . LEU J  3 127 ? 64.313  62.698  151.085 1.00 50.46 ? 127  LEU B CD2   1 
ATOM   4131  N  N     . ALA J  3 128 ? 60.058  65.438  149.253 1.00 39.47 ? 128  ALA B N     1 
ATOM   4132  C  CA    . ALA J  3 128 ? 58.914  65.575  148.367 1.00 38.62 ? 128  ALA B CA    1 
ATOM   4133  C  C     . ALA J  3 128 ? 59.324  66.254  147.072 1.00 38.15 ? 128  ALA B C     1 
ATOM   4134  O  O     . ALA J  3 128 ? 58.707  66.057  146.021 1.00 38.89 ? 128  ALA B O     1 
ATOM   4135  C  CB    . ALA J  3 128 ? 57.814  66.378  149.060 1.00 41.84 ? 128  ALA B CB    1 
ATOM   4136  N  N     . ALA J  3 129 ? 60.380  67.054  147.141 1.00 37.27 ? 129  ALA B N     1 
ATOM   4137  C  CA    . ALA J  3 129 ? 60.844  67.763  145.962 1.00 35.75 ? 129  ALA B CA    1 
ATOM   4138  C  C     . ALA J  3 129 ? 61.321  66.756  144.929 1.00 36.51 ? 129  ALA B C     1 
ATOM   4139  O  O     . ALA J  3 129 ? 61.059  66.901  143.726 1.00 33.66 ? 129  ALA B O     1 
ATOM   4140  C  CB    . ALA J  3 129 ? 61.983  68.717  146.335 1.00 33.27 ? 129  ALA B CB    1 
ATOM   4141  N  N     . ALA J  3 130 ? 62.001  65.718  145.414 1.00 36.72 ? 130  ALA B N     1 
ATOM   4142  C  CA    . ALA J  3 130 ? 62.544  64.689  144.533 1.00 39.26 ? 130  ALA B CA    1 
ATOM   4143  C  C     . ALA J  3 130 ? 61.563  63.574  144.228 1.00 38.28 ? 130  ALA B C     1 
ATOM   4144  O  O     . ALA J  3 130 ? 61.456  63.120  143.081 1.00 40.22 ? 130  ALA B O     1 
ATOM   4145  C  CB    . ALA J  3 130 ? 63.825  64.100  145.153 1.00 39.19 ? 130  ALA B CB    1 
ATOM   4146  N  N     . LEU J  3 131 ? 60.848  63.125  145.251 1.00 38.08 ? 131  LEU B N     1 
ATOM   4147  C  CA    . LEU J  3 131 ? 59.906  62.026  145.080 1.00 41.54 ? 131  LEU B CA    1 
ATOM   4148  C  C     . LEU J  3 131 ? 58.689  62.430  144.274 1.00 44.54 ? 131  LEU B C     1 
ATOM   4149  O  O     . LEU J  3 131 ? 58.115  61.610  143.554 1.00 45.51 ? 131  LEU B O     1 
ATOM   4150  C  CB    . LEU J  3 131 ? 59.468  61.486  146.444 1.00 40.78 ? 131  LEU B CB    1 
ATOM   4151  C  CG    . LEU J  3 131 ? 60.621  61.047  147.354 1.00 42.40 ? 131  LEU B CG    1 
ATOM   4152  C  CD1   . LEU J  3 131 ? 60.110  60.788  148.762 1.00 43.93 ? 131  LEU B CD1   1 
ATOM   4153  C  CD2   . LEU J  3 131 ? 61.280  59.803  146.770 1.00 42.55 ? 131  LEU B CD2   1 
ATOM   4154  N  N     . GLY J  3 132 ? 58.296  63.693  144.383 1.00 45.79 ? 132  GLY B N     1 
ATOM   4155  C  CA    . GLY J  3 132 ? 57.131  64.144  143.654 1.00 46.86 ? 132  GLY B CA    1 
ATOM   4156  C  C     . GLY J  3 132 ? 55.931  63.972  144.556 1.00 46.98 ? 132  GLY B C     1 
ATOM   4157  O  O     . GLY J  3 132 ? 56.093  63.780  145.760 1.00 45.11 ? 132  GLY B O     1 
ATOM   4158  N  N     . SER J  3 133 ? 54.734  64.017  143.978 1.00 48.04 ? 133  SER B N     1 
ATOM   4159  C  CA    . SER J  3 133 ? 53.499  63.888  144.746 1.00 50.24 ? 133  SER B CA    1 
ATOM   4160  C  C     . SER J  3 133 ? 52.408  63.168  143.963 1.00 51.42 ? 133  SER B C     1 
ATOM   4161  O  O     . SER J  3 133 ? 51.489  62.584  144.547 1.00 51.27 ? 133  SER B O     1 
ATOM   4162  C  CB    . SER J  3 133 ? 52.992  65.282  145.143 1.00 52.25 ? 133  SER B CB    1 
ATOM   4163  O  OG    . SER J  3 133 ? 51.675  65.236  145.675 1.00 54.58 ? 133  SER B OG    1 
ATOM   4164  N  N     . ASP J  3 134 ? 52.509  63.213  142.638 1.00 51.16 ? 134  ASP B N     1 
ATOM   4165  C  CA    . ASP J  3 134 ? 51.502  62.594  141.783 1.00 49.27 ? 134  ASP B CA    1 
ATOM   4166  C  C     . ASP J  3 134 ? 51.495  61.069  141.854 1.00 48.35 ? 134  ASP B C     1 
ATOM   4167  O  O     . ASP J  3 134 ? 50.538  60.427  141.414 1.00 44.70 ? 134  ASP B O     1 
ATOM   4168  C  CB    . ASP J  3 134 ? 51.683  63.082  140.342 1.00 50.03 ? 134  ASP B CB    1 
ATOM   4169  C  CG    . ASP J  3 134 ? 51.509  64.599  140.220 1.00 53.04 ? 134  ASP B CG    1 
ATOM   4170  O  OD1   . ASP J  3 134 ? 51.223  65.252  141.250 1.00 57.92 ? 134  ASP B OD1   1 
ATOM   4171  O  OD2   . ASP J  3 134 ? 51.654  65.144  139.108 1.00 53.69 ? 134  ASP B OD2   1 
ATOM   4172  N  N     . TYR J  3 135 ? 52.554  60.493  142.425 1.00 48.09 ? 135  TYR B N     1 
ATOM   4173  C  CA    . TYR J  3 135 ? 52.631  59.043  142.562 1.00 47.91 ? 135  TYR B CA    1 
ATOM   4174  C  C     . TYR J  3 135 ? 51.472  58.595  143.444 1.00 49.32 ? 135  TYR B C     1 
ATOM   4175  O  O     . TYR J  3 135 ? 51.228  57.400  143.613 1.00 50.31 ? 135  TYR B O     1 
ATOM   4176  C  CB    . TYR J  3 135 ? 53.979  58.612  143.165 1.00 44.99 ? 135  TYR B CB    1 
ATOM   4177  C  CG    . TYR J  3 135 ? 54.287  59.159  144.545 1.00 44.87 ? 135  TYR B CG    1 
ATOM   4178  C  CD1   . TYR J  3 135 ? 53.597  58.709  145.676 1.00 45.62 ? 135  TYR B CD1   1 
ATOM   4179  C  CD2   . TYR J  3 135 ? 55.301  60.100  144.725 1.00 48.67 ? 135  TYR B CD2   1 
ATOM   4180  C  CE1   . TYR J  3 135 ? 53.918  59.182  146.961 1.00 45.04 ? 135  TYR B CE1   1 
ATOM   4181  C  CE2   . TYR J  3 135 ? 55.630  60.581  145.998 1.00 48.37 ? 135  TYR B CE2   1 
ATOM   4182  C  CZ    . TYR J  3 135 ? 54.934  60.118  147.108 1.00 47.10 ? 135  TYR B CZ    1 
ATOM   4183  O  OH    . TYR J  3 135 ? 55.257  60.606  148.352 1.00 50.13 ? 135  TYR B OH    1 
ATOM   4184  N  N     . THR J  3 136 ? 50.757  59.568  144.003 1.00 49.11 ? 136  THR B N     1 
ATOM   4185  C  CA    . THR J  3 136 ? 49.601  59.270  144.837 1.00 50.62 ? 136  THR B CA    1 
ATOM   4186  C  C     . THR J  3 136 ? 48.320  59.351  144.001 1.00 49.29 ? 136  THR B C     1 
ATOM   4187  O  O     . THR J  3 136 ? 47.218  59.122  144.519 1.00 49.23 ? 136  THR B O     1 
ATOM   4188  C  CB    . THR J  3 136 ? 49.470  60.264  146.014 1.00 51.38 ? 136  THR B CB    1 
ATOM   4189  O  OG1   . THR J  3 136 ? 49.343  61.600  145.505 1.00 50.60 ? 136  THR B OG1   1 
ATOM   4190  C  CG2   . THR J  3 136 ? 50.682  60.161  146.936 1.00 52.69 ? 136  THR B CG2   1 
ATOM   4191  N  N     . ILE J  3 137 ? 48.459  59.674  142.716 1.00 46.31 ? 137  ILE B N     1 
ATOM   4192  C  CA    . ILE J  3 137 ? 47.284  59.789  141.849 1.00 45.96 ? 137  ILE B CA    1 
ATOM   4193  C  C     . ILE J  3 137 ? 46.646  58.435  141.586 1.00 42.74 ? 137  ILE B C     1 
ATOM   4194  O  O     . ILE J  3 137 ? 47.320  57.475  141.217 1.00 46.88 ? 137  ILE B O     1 
ATOM   4195  C  CB    . ILE J  3 137 ? 47.621  60.487  140.491 1.00 46.83 ? 137  ILE B CB    1 
ATOM   4196  C  CG1   . ILE J  3 137 ? 47.809  61.992  140.729 1.00 45.97 ? 137  ILE B CG1   1 
ATOM   4197  C  CG2   . ILE J  3 137 ? 46.501  60.242  139.460 1.00 44.10 ? 137  ILE B CG2   1 
ATOM   4198  C  CD1   . ILE J  3 137 ? 47.865  62.839  139.462 1.00 47.39 ? 137  ILE B CD1   1 
ATOM   4199  N  N     . THR J  3 138 ? 45.334  58.377  141.787 1.00 39.86 ? 138  THR B N     1 
ATOM   4200  C  CA    . THR J  3 138 ? 44.583  57.157  141.592 1.00 36.63 ? 138  THR B CA    1 
ATOM   4201  C  C     . THR J  3 138 ? 43.805  57.272  140.273 1.00 31.18 ? 138  THR B C     1 
ATOM   4202  O  O     . THR J  3 138 ? 43.304  58.338  139.913 1.00 28.54 ? 138  THR B O     1 
ATOM   4203  C  CB    . THR J  3 138 ? 43.640  56.890  142.811 1.00 40.90 ? 138  THR B CB    1 
ATOM   4204  O  OG1   . THR J  3 138 ? 44.420  56.862  144.023 1.00 40.26 ? 138  THR B OG1   1 
ATOM   4205  C  CG2   . THR J  3 138 ? 42.928  55.548  142.663 1.00 41.30 ? 138  THR B CG2   1 
ATOM   4206  N  N     . PRO J  3 139 ? 43.746  56.170  139.522 1.00 28.27 ? 139  PRO B N     1 
ATOM   4207  C  CA    . PRO J  3 139 ? 43.070  56.043  138.225 1.00 24.24 ? 139  PRO B CA    1 
ATOM   4208  C  C     . PRO J  3 139 ? 41.589  56.377  138.334 1.00 24.46 ? 139  PRO B C     1 
ATOM   4209  O  O     . PRO J  3 139 ? 41.034  56.371  139.423 1.00 23.67 ? 139  PRO B O     1 
ATOM   4210  C  CB    . PRO J  3 139 ? 43.280  54.582  137.877 1.00 23.28 ? 139  PRO B CB    1 
ATOM   4211  C  CG    . PRO J  3 139 ? 44.556  54.236  138.592 1.00 28.69 ? 139  PRO B CG    1 
ATOM   4212  C  CD    . PRO J  3 139 ? 44.380  54.899  139.901 1.00 26.76 ? 139  PRO B CD    1 
ATOM   4213  N  N     . ASP J  3 140 ? 40.948  56.645  137.203 1.00 16.09 ? 140  ASP B N     1 
ATOM   4214  C  CA    . ASP J  3 140 ? 39.518  56.959  137.201 1.00 17.09 ? 140  ASP B CA    1 
ATOM   4215  C  C     . ASP J  3 140 ? 38.704  55.753  137.640 1.00 18.10 ? 140  ASP B C     1 
ATOM   4216  O  O     . ASP J  3 140 ? 37.758  55.885  138.407 1.00 19.19 ? 140  ASP B O     1 
ATOM   4217  C  CB    . ASP J  3 140 ? 39.071  57.348  135.798 1.00 18.66 ? 140  ASP B CB    1 
ATOM   4218  C  CG    . ASP J  3 140 ? 39.664  58.649  135.347 1.00 18.45 ? 140  ASP B CG    1 
ATOM   4219  O  OD1   . ASP J  3 140 ? 40.193  59.388  136.194 1.00 17.45 ? 140  ASP B OD1   1 
ATOM   4220  O  OD2   . ASP J  3 140 ? 39.588  58.940  134.147 1.00 19.31 ? 140  ASP B OD2   1 
ATOM   4221  N  N     . ILE J  3 141 ? 39.046  54.587  137.103 1.00 17.02 ? 141  ILE B N     1 
ATOM   4222  C  CA    . ILE J  3 141 ? 38.354  53.350  137.471 1.00 17.02 ? 141  ILE B CA    1 
ATOM   4223  C  C     . ILE J  3 141 ? 39.434  52.300  137.705 1.00 19.27 ? 141  ILE B C     1 
ATOM   4224  O  O     . ILE J  3 141 ? 40.439  52.260  136.990 1.00 17.67 ? 141  ILE B O     1 
ATOM   4225  C  CB    . ILE J  3 141 ? 37.466  52.805  136.335 1.00 18.89 ? 141  ILE B CB    1 
ATOM   4226  C  CG1   . ILE J  3 141 ? 36.348  53.806  135.968 1.00 17.93 ? 141  ILE B CG1   1 
ATOM   4227  C  CG2   . ILE J  3 141 ? 36.888  51.445  136.765 1.00 22.63 ? 141  ILE B CG2   1 
ATOM   4228  C  CD1   . ILE J  3 141 ? 35.681  53.423  134.658 1.00 20.11 ? 141  ILE B CD1   1 
ATOM   4229  N  N     . ILE J  3 142 ? 39.253  51.468  138.721 1.00 16.52 ? 142  ILE B N     1 
ATOM   4230  C  CA    . ILE J  3 142 ? 40.222  50.394  138.955 1.00 16.79 ? 142  ILE B CA    1 
ATOM   4231  C  C     . ILE J  3 142 ? 39.506  49.056  139.022 1.00 16.77 ? 142  ILE B C     1 
ATOM   4232  O  O     . ILE J  3 142 ? 38.325  48.992  139.360 1.00 19.06 ? 142  ILE B O     1 
ATOM   4233  C  CB    . ILE J  3 142 ? 41.031  50.559  140.287 1.00 15.45 ? 142  ILE B CB    1 
ATOM   4234  C  CG1   . ILE J  3 142 ? 40.083  50.670  141.483 1.00 18.91 ? 142  ILE B CG1   1 
ATOM   4235  C  CG2   . ILE J  3 142 ? 41.982  51.747  140.178 1.00 18.53 ? 142  ILE B CG2   1 
ATOM   4236  C  CD1   . ILE J  3 142 ? 40.820  50.777  142.810 1.00 18.46 ? 142  ILE B CD1   1 
ATOM   4237  N  N     . VAL J  3 143 ? 40.205  48.005  138.615 1.00 14.89 ? 143  VAL B N     1 
ATOM   4238  C  CA    . VAL J  3 143 ? 39.706  46.642  138.745 1.00 15.06 ? 143  VAL B CA    1 
ATOM   4239  C  C     . VAL J  3 143 ? 40.734  46.022  139.689 1.00 17.25 ? 143  VAL B C     1 
ATOM   4240  O  O     . VAL J  3 143 ? 41.948  46.170  139.487 1.00 16.12 ? 143  VAL B O     1 
ATOM   4241  C  CB    . VAL J  3 143 ? 39.708  45.874  137.417 1.00 15.68 ? 143  VAL B CB    1 
ATOM   4242  C  CG1   . VAL J  3 143 ? 39.146  44.438  137.655 1.00 17.99 ? 143  VAL B CG1   1 
ATOM   4243  C  CG2   . VAL J  3 143 ? 38.855  46.611  136.382 1.00 16.79 ? 143  VAL B CG2   1 
ATOM   4244  N  N     . THR J  3 144 ? 40.260  45.353  140.739 1.00 18.10 ? 144  THR B N     1 
ATOM   4245  C  CA    . THR J  3 144 ? 41.170  44.748  141.707 1.00 15.85 ? 144  THR B CA    1 
ATOM   4246  C  C     . THR J  3 144 ? 40.785  43.281  141.925 1.00 14.38 ? 144  THR B C     1 
ATOM   4247  O  O     . THR J  3 144 ? 39.657  42.880  141.607 1.00 16.86 ? 144  THR B O     1 
ATOM   4248  C  CB    . THR J  3 144 ? 41.102  45.488  143.078 1.00 17.72 ? 144  THR B CB    1 
ATOM   4249  O  OG1   . THR J  3 144 ? 39.783  45.357  143.625 1.00 21.88 ? 144  THR B OG1   1 
ATOM   4250  C  CG2   . THR J  3 144 ? 41.401  46.969  142.928 1.00 21.81 ? 144  THR B CG2   1 
ATOM   4251  N  N     . ARG J  3 145 ? 41.732  42.503  142.457 1.00 17.14 ? 145  ARG B N     1 
ATOM   4252  C  CA    . ARG J  3 145 ? 41.531  41.076  142.742 1.00 18.92 ? 145  ARG B CA    1 
ATOM   4253  C  C     . ARG J  3 145 ? 41.798  40.810  144.212 1.00 19.63 ? 145  ARG B C     1 
ATOM   4254  O  O     . ARG J  3 145 ? 42.861  41.157  144.712 1.00 18.80 ? 145  ARG B O     1 
ATOM   4255  C  CB    . ARG J  3 145 ? 42.504  40.212  141.910 1.00 19.52 ? 145  ARG B CB    1 
ATOM   4256  C  CG    . ARG J  3 145 ? 42.258  38.726  142.039 1.00 25.89 ? 145  ARG B CG    1 
ATOM   4257  C  CD    . ARG J  3 145 ? 43.284  37.878  141.314 1.00 26.87 ? 145  ARG B CD    1 
ATOM   4258  N  NE    . ARG J  3 145 ? 42.887  36.479  141.380 1.00 24.46 ? 145  ARG B NE    1 
ATOM   4259  C  CZ    . ARG J  3 145 ? 43.426  35.511  140.660 1.00 25.66 ? 145  ARG B CZ    1 
ATOM   4260  N  NH1   . ARG J  3 145 ? 44.396  35.780  139.808 1.00 24.17 ? 145  ARG B NH1   1 
ATOM   4261  N  NH2   . ARG J  3 145 ? 42.992  34.262  140.794 1.00 26.35 ? 145  ARG B NH2   1 
ATOM   4262  N  N     . ASN J  3 146 ? 40.845  40.198  144.909 1.00 19.42 ? 146  ASN B N     1 
ATOM   4263  C  CA    . ASN J  3 146 ? 41.085  39.866  146.313 1.00 20.90 ? 146  ASN B CA    1 
ATOM   4264  C  C     . ASN J  3 146 ? 42.026  38.665  146.333 1.00 20.38 ? 146  ASN B C     1 
ATOM   4265  O  O     . ASN J  3 146 ? 42.127  37.922  145.350 1.00 20.83 ? 146  ASN B O     1 
ATOM   4266  C  CB    . ASN J  3 146 ? 39.777  39.504  147.012 1.00 24.14 ? 146  ASN B CB    1 
ATOM   4267  C  CG    . ASN J  3 146 ? 38.956  40.717  147.358 1.00 34.16 ? 146  ASN B CG    1 
ATOM   4268  O  OD1   . ASN J  3 146 ? 37.731  40.631  147.526 1.00 35.90 ? 146  ASN B OD1   1 
ATOM   4269  N  ND2   . ASN J  3 146 ? 39.624  41.865  147.482 1.00 28.99 ? 146  ASN B ND2   1 
ATOM   4270  N  N     . LEU J  3 147 ? 42.733  38.487  147.440 1.00 20.28 ? 147  LEU B N     1 
ATOM   4271  C  CA    . LEU J  3 147 ? 43.651  37.372  147.551 1.00 21.23 ? 147  LEU B CA    1 
ATOM   4272  C  C     . LEU J  3 147 ? 42.893  36.043  147.647 1.00 24.36 ? 147  LEU B C     1 
ATOM   4273  O  O     . LEU J  3 147 ? 41.690  36.020  147.903 1.00 25.76 ? 147  LEU B O     1 
ATOM   4274  C  CB    . LEU J  3 147 ? 44.592  37.595  148.747 1.00 20.65 ? 147  LEU B CB    1 
ATOM   4275  C  CG    . LEU J  3 147 ? 45.405  38.895  148.636 1.00 26.04 ? 147  LEU B CG    1 
ATOM   4276  C  CD1   . LEU J  3 147 ? 46.445  38.966  149.723 1.00 25.74 ? 147  LEU B CD1   1 
ATOM   4277  C  CD2   . LEU J  3 147 ? 46.070  38.982  147.279 1.00 27.16 ? 147  LEU B CD2   1 
ATOM   4278  N  N     . ILE J  3 148 ? 43.600  34.936  147.430 1.00 24.99 ? 148  ILE B N     1 
ATOM   4279  C  CA    . ILE J  3 148 ? 42.988  33.610  147.437 1.00 25.07 ? 148  ILE B CA    1 
ATOM   4280  C  C     . ILE J  3 148 ? 43.326  32.792  148.692 1.00 24.29 ? 148  ILE B C     1 
ATOM   4281  O  O     . ILE J  3 148 ? 44.446  32.827  149.185 1.00 24.49 ? 148  ILE B O     1 
ATOM   4282  C  CB    . ILE J  3 148 ? 43.467  32.813  146.216 1.00 25.80 ? 148  ILE B CB    1 
ATOM   4283  C  CG1   . ILE J  3 148 ? 43.200  33.613  144.940 1.00 31.34 ? 148  ILE B CG1   1 
ATOM   4284  C  CG2   . ILE J  3 148 ? 42.768  31.474  146.138 1.00 32.25 ? 148  ILE B CG2   1 
ATOM   4285  C  CD1   . ILE J  3 148 ? 43.788  32.949  143.705 1.00 31.62 ? 148  ILE B CD1   1 
ATOM   4286  N  N     . ALA J  3 149 ? 42.354  32.043  149.200 1.00 23.47 ? 149  ALA B N     1 
ATOM   4287  C  CA    . ALA J  3 149 ? 42.626  31.216  150.378 1.00 22.37 ? 149  ALA B CA    1 
ATOM   4288  C  C     . ALA J  3 149 ? 43.442  29.994  149.976 1.00 20.63 ? 149  ALA B C     1 
ATOM   4289  O  O     . ALA J  3 149 ? 43.357  29.529  148.843 1.00 19.71 ? 149  ALA B O     1 
ATOM   4290  C  CB    . ALA J  3 149 ? 41.296  30.756  151.013 1.00 26.97 ? 149  ALA B CB    1 
ATOM   4291  N  N     . ASP J  3 150 ? 44.224  29.453  150.907 1.00 20.94 ? 150  ASP B N     1 
ATOM   4292  C  CA    . ASP J  3 150 ? 44.987  28.250  150.602 1.00 21.01 ? 150  ASP B CA    1 
ATOM   4293  C  C     . ASP J  3 150 ? 44.036  27.120  150.199 1.00 17.16 ? 150  ASP B C     1 
ATOM   4294  O  O     . ASP J  3 150 ? 44.390  26.246  149.410 1.00 19.68 ? 150  ASP B O     1 
ATOM   4295  C  CB    . ASP J  3 150 ? 45.835  27.837  151.805 1.00 19.62 ? 150  ASP B CB    1 
ATOM   4296  C  CG    . ASP J  3 150 ? 47.066  28.711  151.970 1.00 25.16 ? 150  ASP B CG    1 
ATOM   4297  O  OD1   . ASP J  3 150 ? 47.328  29.549  151.078 1.00 25.69 ? 150  ASP B OD1   1 
ATOM   4298  O  OD2   . ASP J  3 150 ? 47.766  28.564  152.991 1.00 23.49 ? 150  ASP B OD2   1 
ATOM   4299  N  N     . ALA J  3 151 ? 42.818  27.153  150.735 1.00 18.46 ? 151  ALA B N     1 
ATOM   4300  C  CA    . ALA J  3 151 ? 41.806  26.155  150.417 1.00 19.88 ? 151  ALA B CA    1 
ATOM   4301  C  C     . ALA J  3 151 ? 41.564  26.081  148.912 1.00 20.11 ? 151  ALA B C     1 
ATOM   4302  O  O     . ALA J  3 151 ? 41.368  24.996  148.368 1.00 22.82 ? 151  ALA B O     1 
ATOM   4303  C  CB    . ALA J  3 151 ? 40.502  26.492  151.118 1.00 18.72 ? 151  ALA B CB    1 
ATOM   4304  N  N     . GLU J  3 152 ? 41.572  27.240  148.242 1.00 19.91 ? 152  GLU B N     1 
ATOM   4305  C  CA    . GLU J  3 152 ? 41.337  27.274  146.791 1.00 21.80 ? 152  GLU B CA    1 
ATOM   4306  C  C     . GLU J  3 152 ? 42.607  26.875  146.028 1.00 19.74 ? 152  GLU B C     1 
ATOM   4307  O  O     . GLU J  3 152 ? 42.538  26.163  145.021 1.00 20.64 ? 152  GLU B O     1 
ATOM   4308  C  CB    . GLU J  3 152 ? 40.832  28.671  146.380 1.00 25.99 ? 152  GLU B CB    1 
ATOM   4309  C  CG    . GLU J  3 152 ? 40.493  28.863  144.893 1.00 32.92 ? 152  GLU B CG    1 
ATOM   4310  C  CD    . GLU J  3 152 ? 39.567  27.792  144.324 1.00 39.04 ? 152  GLU B CD    1 
ATOM   4311  O  OE1   . GLU J  3 152 ? 38.680  27.293  145.056 1.00 41.89 ? 152  GLU B OE1   1 
ATOM   4312  O  OE2   . GLU J  3 152 ? 39.713  27.453  143.127 1.00 38.75 ? 152  GLU B OE2   1 
ATOM   4313  N  N     . ILE J  3 153 ? 43.766  27.323  146.509 1.00 19.57 ? 153  ILE B N     1 
ATOM   4314  C  CA    . ILE J  3 153 ? 45.009  26.932  145.854 1.00 19.35 ? 153  ILE B CA    1 
ATOM   4315  C  C     . ILE J  3 153 ? 45.105  25.407  145.903 1.00 20.26 ? 153  ILE B C     1 
ATOM   4316  O  O     . ILE J  3 153 ? 45.443  24.752  144.915 1.00 19.18 ? 153  ILE B O     1 
ATOM   4317  C  CB    . ILE J  3 153 ? 46.241  27.578  146.548 1.00 19.26 ? 153  ILE B CB    1 
ATOM   4318  C  CG1   . ILE J  3 153 ? 46.183  29.102  146.370 1.00 21.02 ? 153  ILE B CG1   1 
ATOM   4319  C  CG2   . ILE J  3 153 ? 47.537  26.984  146.001 1.00 16.98 ? 153  ILE B CG2   1 
ATOM   4320  C  CD1   . ILE J  3 153 ? 47.225  29.857  147.186 1.00 22.50 ? 153  ILE B CD1   1 
ATOM   4321  N  N     . ASN J  3 154 ? 44.728  24.837  147.051 1.00 20.51 ? 154  ASN B N     1 
ATOM   4322  C  CA    . ASN J  3 154 ? 44.781  23.378  147.239 1.00 18.71 ? 154  ASN B CA    1 
ATOM   4323  C  C     . ASN J  3 154 ? 43.449  22.676  146.920 1.00 22.03 ? 154  ASN B C     1 
ATOM   4324  O  O     . ASN J  3 154 ? 43.172  21.590  147.441 1.00 19.92 ? 154  ASN B O     1 
ATOM   4325  C  CB    . ASN J  3 154 ? 45.162  23.070  148.700 1.00 19.15 ? 154  ASN B CB    1 
ATOM   4326  C  CG    . ASN J  3 154 ? 46.567  23.554  149.051 1.00 21.39 ? 154  ASN B CG    1 
ATOM   4327  O  OD1   . ASN J  3 154 ? 47.479  23.509  148.212 1.00 20.84 ? 154  ASN B OD1   1 
ATOM   4328  N  ND2   . ASN J  3 154 ? 46.755  23.984  150.295 1.00 19.87 ? 154  ASN B ND2   1 
ATOM   4329  N  N     . ARG J  3 155 ? 42.635  23.266  146.049 1.00 19.45 ? 155  ARG B N     1 
ATOM   4330  C  CA    . ARG J  3 155 ? 41.333  22.672  145.735 1.00 22.20 ? 155  ARG B CA    1 
ATOM   4331  C  C     . ARG J  3 155 ? 41.351  21.233  145.241 1.00 22.89 ? 155  ARG B C     1 
ATOM   4332  O  O     . ARG J  3 155 ? 40.496  20.424  145.625 1.00 22.92 ? 155  ARG B O     1 
ATOM   4333  C  CB    . ARG J  3 155 ? 40.567  23.544  144.714 1.00 23.11 ? 155  ARG B CB    1 
ATOM   4334  C  CG    . ARG J  3 155 ? 39.219  22.915  144.288 1.00 25.77 ? 155  ARG B CG    1 
ATOM   4335  C  CD    . ARG J  3 155 ? 38.429  23.770  143.282 1.00 29.77 ? 155  ARG B CD    1 
ATOM   4336  N  NE    . ARG J  3 155 ? 37.458  24.626  143.969 1.00 37.43 ? 155  ARG B NE    1 
ATOM   4337  C  CZ    . ARG J  3 155 ? 36.175  24.315  144.142 1.00 29.98 ? 155  ARG B CZ    1 
ATOM   4338  N  NH1   . ARG J  3 155 ? 35.698  23.176  143.670 1.00 28.13 ? 155  ARG B NH1   1 
ATOM   4339  N  NH2   . ARG J  3 155 ? 35.374  25.139  144.809 1.00 37.55 ? 155  ARG B NH2   1 
ATOM   4340  N  N     . ASN J  3 156 ? 42.319  20.892  144.401 1.00 23.00 ? 156  ASN B N     1 
ATOM   4341  C  CA    . ASN J  3 156 ? 42.384  19.559  143.839 1.00 24.97 ? 156  ASN B CA    1 
ATOM   4342  C  C     . ASN J  3 156 ? 43.544  18.718  144.337 1.00 27.16 ? 156  ASN B C     1 
ATOM   4343  O  O     . ASN J  3 156 ? 43.468  17.486  144.338 1.00 27.48 ? 156  ASN B O     1 
ATOM   4344  C  CB    . ASN J  3 156 ? 42.451  19.651  142.314 1.00 26.58 ? 156  ASN B CB    1 
ATOM   4345  C  CG    . ASN J  3 156 ? 41.294  20.445  141.728 1.00 31.46 ? 156  ASN B CG    1 
ATOM   4346  O  OD1   . ASN J  3 156 ? 40.133  20.243  142.094 1.00 31.74 ? 156  ASN B OD1   1 
ATOM   4347  N  ND2   . ASN J  3 156 ? 41.605  21.347  140.810 1.00 31.94 ? 156  ASN B ND2   1 
ATOM   4348  N  N     . GLU J  3 157 ? 44.622  19.378  144.740 1.00 25.91 ? 157  GLU B N     1 
ATOM   4349  C  CA    . GLU J  3 157 ? 45.817  18.687  145.217 1.00 24.46 ? 157  GLU B CA    1 
ATOM   4350  C  C     . GLU J  3 157 ? 46.421  19.511  146.344 1.00 19.77 ? 157  GLU B C     1 
ATOM   4351  O  O     . GLU J  3 157 ? 46.177  20.705  146.447 1.00 19.46 ? 157  GLU B O     1 
ATOM   4352  C  CB    . GLU J  3 157 ? 46.863  18.565  144.093 1.00 28.73 ? 157  GLU B CB    1 
ATOM   4353  C  CG    . GLU J  3 157 ? 46.297  18.124  142.772 1.00 32.70 ? 157  GLU B CG    1 
ATOM   4354  C  CD    . GLU J  3 157 ? 47.327  18.121  141.673 1.00 34.00 ? 157  GLU B CD    1 
ATOM   4355  O  OE1   . GLU J  3 157 ? 48.114  17.162  141.609 1.00 32.90 ? 157  GLU B OE1   1 
ATOM   4356  O  OE2   . GLU J  3 157 ? 47.364  19.086  140.877 1.00 32.93 ? 157  GLU B OE2   1 
ATOM   4357  N  N     . PHE J  3 158 ? 47.240  18.864  147.170 1.00 20.29 ? 158  PHE B N     1 
ATOM   4358  C  CA    . PHE J  3 158 ? 47.896  19.536  148.281 1.00 19.16 ? 158  PHE B CA    1 
ATOM   4359  C  C     . PHE J  3 158 ? 49.170  20.178  147.719 1.00 20.24 ? 158  PHE B C     1 
ATOM   4360  O  O     . PHE J  3 158 ? 50.254  19.568  147.698 1.00 20.88 ? 158  PHE B O     1 
ATOM   4361  C  CB    . PHE J  3 158 ? 48.216  18.493  149.356 1.00 23.55 ? 158  PHE B CB    1 
ATOM   4362  C  CG    . PHE J  3 158 ? 48.890  19.048  150.574 1.00 23.46 ? 158  PHE B CG    1 
ATOM   4363  C  CD1   . PHE J  3 158 ? 48.576  20.314  151.058 1.00 24.07 ? 158  PHE B CD1   1 
ATOM   4364  C  CD2   . PHE J  3 158 ? 49.807  18.275  151.266 1.00 27.71 ? 158  PHE B CD2   1 
ATOM   4365  C  CE1   . PHE J  3 158 ? 49.167  20.800  152.223 1.00 26.24 ? 158  PHE B CE1   1 
ATOM   4366  C  CE2   . PHE J  3 158 ? 50.404  18.749  152.430 1.00 27.61 ? 158  PHE B CE2   1 
ATOM   4367  C  CZ    . PHE J  3 158 ? 50.084  20.011  152.910 1.00 25.62 ? 158  PHE B CZ    1 
ATOM   4368  N  N     . LEU J  3 159 ? 49.026  21.421  147.271 1.00 20.16 ? 159  LEU B N     1 
ATOM   4369  C  CA    . LEU J  3 159 ? 50.137  22.159  146.660 1.00 18.97 ? 159  LEU B CA    1 
ATOM   4370  C  C     . LEU J  3 159 ? 51.026  22.945  147.598 1.00 19.07 ? 159  LEU B C     1 
ATOM   4371  O  O     . LEU J  3 159 ? 52.243  22.968  147.421 1.00 19.05 ? 159  LEU B O     1 
ATOM   4372  C  CB    . LEU J  3 159 ? 49.584  23.137  145.614 1.00 20.53 ? 159  LEU B CB    1 
ATOM   4373  C  CG    . LEU J  3 159 ? 48.765  22.529  144.482 1.00 19.23 ? 159  LEU B CG    1 
ATOM   4374  C  CD1   . LEU J  3 159 ? 48.394  23.660  143.510 1.00 17.42 ? 159  LEU B CD1   1 
ATOM   4375  C  CD2   . LEU J  3 159 ? 49.548  21.444  143.744 1.00 22.25 ? 159  LEU B CD2   1 
ATOM   4376  N  N     . VAL J  3 160 ? 50.420  23.597  148.591 1.00 18.44 ? 160  VAL B N     1 
ATOM   4377  C  CA    . VAL J  3 160 ? 51.165  24.427  149.509 1.00 19.89 ? 160  VAL B CA    1 
ATOM   4378  C  C     . VAL J  3 160 ? 50.734  24.304  150.954 1.00 22.43 ? 160  VAL B C     1 
ATOM   4379  O  O     . VAL J  3 160 ? 49.599  23.921  151.248 1.00 22.59 ? 160  VAL B O     1 
ATOM   4380  C  CB    . VAL J  3 160 ? 51.024  25.934  149.138 1.00 19.47 ? 160  VAL B CB    1 
ATOM   4381  C  CG1   . VAL J  3 160 ? 51.458  26.155  147.674 1.00 21.71 ? 160  VAL B CG1   1 
ATOM   4382  C  CG2   . VAL J  3 160 ? 49.558  26.419  149.357 1.00 19.52 ? 160  VAL B CG2   1 
ATOM   4383  N  N     . ASP J  3 161 ? 51.666  24.631  151.846 1.00 21.89 ? 161  ASP B N     1 
ATOM   4384  C  CA    . ASP J  3 161 ? 51.392  24.692  153.279 1.00 26.05 ? 161  ASP B CA    1 
ATOM   4385  C  C     . ASP J  3 161 ? 52.121  25.939  153.754 1.00 26.44 ? 161  ASP B C     1 
ATOM   4386  O  O     . ASP J  3 161 ? 52.543  26.753  152.923 1.00 23.14 ? 161  ASP B O     1 
ATOM   4387  C  CB    . ASP J  3 161 ? 51.782  23.408  154.053 1.00 26.12 ? 161  ASP B CB    1 
ATOM   4388  C  CG    . ASP J  3 161 ? 53.271  23.123  154.084 1.00 28.04 ? 161  ASP B CG    1 
ATOM   4389  O  OD1   . ASP J  3 161 ? 54.088  23.928  153.586 1.00 22.60 ? 161  ASP B OD1   1 
ATOM   4390  O  OD2   . ASP J  3 161 ? 53.616  22.052  154.634 1.00 29.74 ? 161  ASP B OD2   1 
ATOM   4391  N  N     . GLU J  3 162 ? 52.277  26.122  155.058 1.00 23.27 ? 162  GLU B N     1 
ATOM   4392  C  CA    . GLU J  3 162 ? 52.881  27.348  155.562 1.00 23.81 ? 162  GLU B CA    1 
ATOM   4393  C  C     . GLU J  3 162 ? 54.405  27.482  155.426 1.00 21.44 ? 162  GLU B C     1 
ATOM   4394  O  O     . GLU J  3 162 ? 54.965  28.518  155.789 1.00 23.49 ? 162  GLU B O     1 
ATOM   4395  C  CB    . GLU J  3 162 ? 52.480  27.535  157.032 1.00 28.87 ? 162  GLU B CB    1 
ATOM   4396  C  CG    . GLU J  3 162 ? 53.057  26.501  158.008 1.00 35.18 ? 162  GLU B CG    1 
ATOM   4397  C  CD    . GLU J  3 162 ? 52.438  25.099  157.910 1.00 42.32 ? 162  GLU B CD    1 
ATOM   4398  O  OE1   . GLU J  3 162 ? 51.361  24.924  157.285 1.00 39.60 ? 162  GLU B OE1   1 
ATOM   4399  O  OE2   . GLU J  3 162 ? 53.039  24.158  158.487 1.00 44.35 ? 162  GLU B OE2   1 
ATOM   4400  N  N     . ASN J  3 163 ? 55.058  26.453  154.894 1.00 19.48 ? 163  ASN B N     1 
ATOM   4401  C  CA    . ASN J  3 163 ? 56.509  26.486  154.779 1.00 21.13 ? 163  ASN B CA    1 
ATOM   4402  C  C     . ASN J  3 163 ? 57.038  26.483  153.362 1.00 21.75 ? 163  ASN B C     1 
ATOM   4403  O  O     . ASN J  3 163 ? 58.225  26.235  153.138 1.00 22.45 ? 163  ASN B O     1 
ATOM   4404  C  CB    . ASN J  3 163 ? 57.108  25.309  155.543 1.00 23.80 ? 163  ASN B CB    1 
ATOM   4405  C  CG    . ASN J  3 163 ? 56.762  25.354  157.026 1.00 23.02 ? 163  ASN B CG    1 
ATOM   4406  O  OD1   . ASN J  3 163 ? 56.964  26.374  157.684 1.00 31.95 ? 163  ASN B OD1   1 
ATOM   4407  N  ND2   . ASN J  3 163 ? 56.237  24.250  157.549 1.00 29.86 ? 163  ASN B ND2   1 
ATOM   4408  N  N     . ILE J  3 164 ? 56.161  26.735  152.406 1.00 19.14 ? 164  ILE B N     1 
ATOM   4409  C  CA    . ILE J  3 164 ? 56.581  26.762  150.993 1.00 18.34 ? 164  ILE B CA    1 
ATOM   4410  C  C     . ILE J  3 164 ? 55.808  27.895  150.315 1.00 17.11 ? 164  ILE B C     1 
ATOM   4411  O  O     . ILE J  3 164 ? 54.694  28.208  150.720 1.00 19.44 ? 164  ILE B O     1 
ATOM   4412  C  CB    . ILE J  3 164 ? 56.275  25.398  150.317 1.00 19.60 ? 164  ILE B CB    1 
ATOM   4413  C  CG1   . ILE J  3 164 ? 56.903  25.326  148.918 1.00 17.81 ? 164  ILE B CG1   1 
ATOM   4414  C  CG2   . ILE J  3 164 ? 54.738  25.147  150.272 1.00 18.78 ? 164  ILE B CG2   1 
ATOM   4415  C  CD1   . ILE J  3 164 ? 58.446  25.250  148.908 1.00 20.00 ? 164  ILE B CD1   1 
ATOM   4416  N  N     . ALA J  3 165 ? 56.406  28.532  149.299 1.00 17.33 ? 165  ALA B N     1 
ATOM   4417  C  CA    . ALA J  3 165 ? 55.747  29.643  148.573 1.00 17.00 ? 165  ALA B CA    1 
ATOM   4418  C  C     . ALA J  3 165 ? 55.142  30.637  149.561 1.00 16.70 ? 165  ALA B C     1 
ATOM   4419  O  O     . ALA J  3 165 ? 53.989  31.085  149.414 1.00 19.01 ? 165  ALA B O     1 
ATOM   4420  C  CB    . ALA J  3 165 ? 54.668  29.080  147.633 1.00 17.57 ? 165  ALA B CB    1 
ATOM   4421  N  N     . THR J  3 166 ? 55.951  31.028  150.542 1.00 15.31 ? 166  THR B N     1 
ATOM   4422  C  CA    . THR J  3 166 ? 55.491  31.892  151.611 1.00 18.17 ? 166  THR B CA    1 
ATOM   4423  C  C     . THR J  3 166 ? 55.351  33.369  151.321 1.00 17.79 ? 166  THR B C     1 
ATOM   4424  O  O     . THR J  3 166 ? 54.826  34.126  152.147 1.00 22.57 ? 166  THR B O     1 
ATOM   4425  C  CB    . THR J  3 166 ? 56.408  31.715  152.847 1.00 19.76 ? 166  THR B CB    1 
ATOM   4426  O  OG1   . THR J  3 166 ? 57.706  32.219  152.539 1.00 22.47 ? 166  THR B OG1   1 
ATOM   4427  C  CG2   . THR J  3 166 ? 56.549  30.228  153.182 1.00 25.73 ? 166  THR B CG2   1 
ATOM   4428  N  N     . TYR J  3 167 ? 55.805  33.800  150.149 1.00 14.90 ? 167  TYR B N     1 
ATOM   4429  C  CA    . TYR J  3 167 ? 55.706  35.200  149.801 1.00 16.31 ? 167  TYR B CA    1 
ATOM   4430  C  C     . TYR J  3 167 ? 54.858  35.393  148.558 1.00 14.76 ? 167  TYR B C     1 
ATOM   4431  O  O     . TYR J  3 167 ? 54.812  36.512  148.021 1.00 18.28 ? 167  TYR B O     1 
ATOM   4432  C  CB    . TYR J  3 167 ? 57.094  35.806  149.524 1.00 18.48 ? 167  TYR B CB    1 
ATOM   4433  C  CG    . TYR J  3 167 ? 58.017  35.747  150.712 1.00 21.98 ? 167  TYR B CG    1 
ATOM   4434  C  CD1   . TYR J  3 167 ? 59.122  34.910  150.698 1.00 17.75 ? 167  TYR B CD1   1 
ATOM   4435  C  CD2   . TYR J  3 167 ? 57.758  36.503  151.860 1.00 22.10 ? 167  TYR B CD2   1 
ATOM   4436  C  CE1   . TYR J  3 167 ? 59.966  34.817  151.805 1.00 22.60 ? 167  TYR B CE1   1 
ATOM   4437  C  CE2   . TYR J  3 167 ? 58.597  36.414  152.979 1.00 26.00 ? 167  TYR B CE2   1 
ATOM   4438  C  CZ    . TYR J  3 167 ? 59.699  35.562  152.930 1.00 23.73 ? 167  TYR B CZ    1 
ATOM   4439  O  OH    . TYR J  3 167 ? 60.542  35.435  154.018 1.00 30.06 ? 167  TYR B OH    1 
ATOM   4440  N  N     . ALA J  3 168 ? 54.177  34.333  148.128 1.00 15.74 ? 168  ALA B N     1 
ATOM   4441  C  CA    . ALA J  3 168 ? 53.350  34.404  146.918 1.00 15.33 ? 168  ALA B CA    1 
ATOM   4442  C  C     . ALA J  3 168 ? 52.329  35.532  147.079 1.00 19.78 ? 168  ALA B C     1 
ATOM   4443  O  O     . ALA J  3 168 ? 51.629  35.625  148.082 1.00 18.00 ? 168  ALA B O     1 
ATOM   4444  C  CB    . ALA J  3 168 ? 52.658  33.091  146.690 1.00 15.19 ? 168  ALA B CB    1 
ATOM   4445  N  N     . SER J  3 169 ? 52.241  36.395  146.074 1.00 16.15 ? 169  SER B N     1 
ATOM   4446  C  CA    . SER J  3 169 ? 51.340  37.536  146.126 1.00 16.69 ? 169  SER B CA    1 
ATOM   4447  C  C     . SER J  3 169 ? 49.869  37.182  146.320 1.00 16.25 ? 169  SER B C     1 
ATOM   4448  O  O     . SER J  3 169 ? 49.137  37.928  146.955 1.00 20.29 ? 169  SER B O     1 
ATOM   4449  C  CB    . SER J  3 169 ? 51.450  38.349  144.829 1.00 18.72 ? 169  SER B CB    1 
ATOM   4450  O  OG    . SER J  3 169 ? 52.790  38.778  144.603 1.00 23.51 ? 169  SER B OG    1 
ATOM   4451  N  N     . LEU J  3 170 ? 49.432  36.073  145.751 1.00 15.77 ? 170  LEU B N     1 
ATOM   4452  C  CA    . LEU J  3 170 ? 48.021  35.707  145.838 1.00 15.24 ? 170  LEU B CA    1 
ATOM   4453  C  C     . LEU J  3 170 ? 47.603  35.133  147.162 1.00 19.53 ? 170  LEU B C     1 
ATOM   4454  O  O     . LEU J  3 170 ? 46.409  35.007  147.396 1.00 22.62 ? 170  LEU B O     1 
ATOM   4455  C  CB    . LEU J  3 170 ? 47.653  34.707  144.749 1.00 18.37 ? 170  LEU B CB    1 
ATOM   4456  C  CG    . LEU J  3 170 ? 47.569  35.258  143.323 1.00 17.88 ? 170  LEU B CG    1 
ATOM   4457  C  CD1   . LEU J  3 170 ? 47.617  34.118  142.320 1.00 18.70 ? 170  LEU B CD1   1 
ATOM   4458  C  CD2   . LEU J  3 170 ? 46.287  36.070  143.177 1.00 16.72 ? 170  LEU B CD2   1 
ATOM   4459  N  N     . ARG J  3 171 ? 48.559  34.783  148.020 1.00 22.22 ? 171  ARG B N     1 
ATOM   4460  C  CA    . ARG J  3 171 ? 48.200  34.182  149.296 1.00 24.02 ? 171  ARG B CA    1 
ATOM   4461  C  C     . ARG J  3 171 ? 47.815  35.195  150.340 1.00 28.67 ? 171  ARG B C     1 
ATOM   4462  O  O     . ARG J  3 171 ? 48.555  36.130  150.647 1.00 24.71 ? 171  ARG B O     1 
ATOM   4463  C  CB    . ARG J  3 171 ? 49.318  33.271  149.804 1.00 23.01 ? 171  ARG B CB    1 
ATOM   4464  C  CG    . ARG J  3 171 ? 49.475  32.040  148.946 1.00 20.59 ? 171  ARG B CG    1 
ATOM   4465  C  CD    . ARG J  3 171 ? 50.579  31.117  149.454 1.00 22.13 ? 171  ARG B CD    1 
ATOM   4466  N  NE    . ARG J  3 171 ? 50.132  30.281  150.563 1.00 19.60 ? 171  ARG B NE    1 
ATOM   4467  C  CZ    . ARG J  3 171 ? 50.914  29.377  151.144 1.00 22.88 ? 171  ARG B CZ    1 
ATOM   4468  N  NH1   . ARG J  3 171 ? 52.158  29.225  150.712 1.00 22.40 ? 171  ARG B NH1   1 
ATOM   4469  N  NH2   . ARG J  3 171 ? 50.455  28.609  152.131 1.00 20.46 ? 171  ARG B NH2   1 
ATOM   4470  N  N     . ALA J  3 172 ? 46.594  35.007  150.825 1.00 37.03 ? 172  ALA B N     1 
ATOM   4471  C  CA    . ALA J  3 172 ? 46.003  35.851  151.842 1.00 43.97 ? 172  ALA B CA    1 
ATOM   4472  C  C     . ALA J  3 172 ? 46.800  35.553  153.099 1.00 48.54 ? 172  ALA B C     1 
ATOM   4473  O  O     . ALA J  3 172 ? 46.355  34.799  153.958 1.00 51.48 ? 172  ALA B O     1 
ATOM   4474  C  CB    . ALA J  3 172 ? 44.523  35.476  152.025 1.00 41.47 ? 172  ALA B CB    1 
ATOM   4475  N  N     . GLY J  3 173 ? 47.995  36.133  153.177 1.00 52.60 ? 173  GLY B N     1 
ATOM   4476  C  CA    . GLY J  3 173 ? 48.858  35.904  154.314 1.00 56.37 ? 173  GLY B CA    1 
ATOM   4477  C  C     . GLY J  3 173 ? 49.686  37.097  154.762 1.00 58.90 ? 173  GLY B C     1 
ATOM   4478  O  O     . GLY J  3 173 ? 49.326  37.759  155.733 1.00 60.04 ? 173  GLY B O     1 
ATOM   4479  N  N     . ASN J  3 174 ? 50.788  37.372  154.061 1.00 60.04 ? 174  ASN B N     1 
ATOM   4480  C  CA    . ASN J  3 174 ? 51.703  38.473  154.411 1.00 60.04 ? 174  ASN B CA    1 
ATOM   4481  C  C     . ASN J  3 174 ? 51.082  39.860  154.584 1.00 60.04 ? 174  ASN B C     1 
ATOM   4482  O  O     . ASN J  3 174 ? 51.579  40.839  154.001 1.00 60.04 ? 174  ASN B O     1 
ATOM   4483  C  CB    . ASN J  3 174 ? 52.832  38.569  153.372 1.00 60.04 ? 174  ASN B CB    1 
ATOM   4484  C  CG    . ASN J  3 174 ? 54.149  38.018  153.892 1.00 60.04 ? 174  ASN B CG    1 
ATOM   4485  O  OD1   . ASN J  3 174 ? 55.142  37.972  153.175 1.00 60.04 ? 174  ASN B OD1   1 
ATOM   4486  N  ND2   . ASN J  3 174 ? 54.159  37.600  155.153 1.00 60.04 ? 174  ASN B ND2   1 
ATOM   4487  N  N     . GLY J  3 175 ? 50.027  39.951  155.399 1.00 60.04 ? 175  GLY B N     1 
ATOM   4488  C  CA    . GLY J  3 175 ? 49.350  41.221  155.607 1.00 60.04 ? 175  GLY B CA    1 
ATOM   4489  C  C     . GLY J  3 175 ? 49.015  41.783  154.238 1.00 58.15 ? 175  GLY B C     1 
ATOM   4490  O  O     . GLY J  3 175 ? 48.421  42.853  154.098 1.00 59.89 ? 175  GLY B O     1 
ATOM   4491  N  N     . ASN J  3 176 ? 49.411  41.015  153.229 1.00 55.95 ? 176  ASN B N     1 
ATOM   4492  C  CA    . ASN J  3 176 ? 49.225  41.356  151.837 1.00 51.94 ? 176  ASN B CA    1 
ATOM   4493  C  C     . ASN J  3 176 ? 47.830  41.900  151.570 1.00 46.11 ? 176  ASN B C     1 
ATOM   4494  O  O     . ASN J  3 176 ? 46.841  41.463  152.166 1.00 44.89 ? 176  ASN B O     1 
ATOM   4495  C  CB    . ASN J  3 176 ? 49.484  40.128  150.974 1.00 54.85 ? 176  ASN B CB    1 
ATOM   4496  C  CG    . ASN J  3 176 ? 49.516  40.465  149.513 1.00 60.04 ? 176  ASN B CG    1 
ATOM   4497  O  OD1   . ASN J  3 176 ? 49.201  41.593  149.116 1.00 60.04 ? 176  ASN B OD1   1 
ATOM   4498  N  ND2   . ASN J  3 176 ? 49.892  39.492  148.690 1.00 60.03 ? 176  ASN B ND2   1 
ATOM   4499  N  N     . MET J  3 177 ? 47.772  42.864  150.670 1.00 41.01 ? 177  MET B N     1 
ATOM   4500  C  CA    . MET J  3 177 ? 46.532  43.508  150.305 1.00 34.61 ? 177  MET B CA    1 
ATOM   4501  C  C     . MET J  3 177 ? 46.100  42.984  148.951 1.00 31.17 ? 177  MET B C     1 
ATOM   4502  O  O     . MET J  3 177 ? 46.836  42.224  148.305 1.00 28.52 ? 177  MET B O     1 
ATOM   4503  C  CB    . MET J  3 177 ? 46.773  45.005  150.228 1.00 38.37 ? 177  MET B CB    1 
ATOM   4504  C  CG    . MET J  3 177 ? 47.289  45.601  151.536 1.00 42.32 ? 177  MET B CG    1 
ATOM   4505  S  SD    . MET J  3 177 ? 48.604  46.782  151.219 1.00 45.71 ? 177  MET B SD    1 
ATOM   4506  C  CE    . MET J  3 177 ? 49.989  45.702  151.241 1.00 38.77 ? 177  MET B CE    1 
ATOM   4507  N  N     . PRO J  3 178 ? 44.890  43.366  148.507 1.00 26.44 ? 178  PRO B N     1 
ATOM   4508  C  CA    . PRO J  3 178 ? 44.411  42.905  147.199 1.00 21.23 ? 178  PRO B CA    1 
ATOM   4509  C  C     . PRO J  3 178 ? 45.347  43.436  146.107 1.00 19.61 ? 178  PRO B C     1 
ATOM   4510  O  O     . PRO J  3 178 ? 46.101  44.384  146.326 1.00 19.88 ? 178  PRO B O     1 
ATOM   4511  C  CB    . PRO J  3 178 ? 43.033  43.547  147.075 1.00 22.06 ? 178  PRO B CB    1 
ATOM   4512  C  CG    . PRO J  3 178 ? 42.606  43.700  148.498 1.00 27.89 ? 178  PRO B CG    1 
ATOM   4513  C  CD    . PRO J  3 178 ? 43.856  44.153  149.199 1.00 25.01 ? 178  PRO B CD    1 
ATOM   4514  N  N     . LEU J  3 179 ? 45.262  42.824  144.934 1.00 17.97 ? 179  LEU B N     1 
ATOM   4515  C  CA    . LEU J  3 179 ? 46.080  43.221  143.806 1.00 16.72 ? 179  LEU B CA    1 
ATOM   4516  C  C     . LEU J  3 179 ? 45.365  44.181  142.864 1.00 16.72 ? 179  LEU B C     1 
ATOM   4517  O  O     . LEU J  3 179 ? 44.158  44.044  142.634 1.00 18.96 ? 179  LEU B O     1 
ATOM   4518  C  CB    . LEU J  3 179 ? 46.497  41.978  143.010 1.00 17.56 ? 179  LEU B CB    1 
ATOM   4519  C  CG    . LEU J  3 179 ? 47.516  41.116  143.758 1.00 21.15 ? 179  LEU B CG    1 
ATOM   4520  C  CD1   . LEU J  3 179 ? 47.330  39.673  143.382 1.00 22.82 ? 179  LEU B CD1   1 
ATOM   4521  C  CD2   . LEU J  3 179 ? 48.938  41.604  143.452 1.00 22.52 ? 179  LEU B CD2   1 
ATOM   4522  N  N     . LEU J  3 180 ? 46.109  45.144  142.318 1.00 15.68 ? 180  LEU B N     1 
ATOM   4523  C  CA    . LEU J  3 180 ? 45.527  46.052  141.331 1.00 14.27 ? 180  LEU B CA    1 
ATOM   4524  C  C     . LEU J  3 180 ? 45.618  45.324  139.978 1.00 14.70 ? 180  LEU B C     1 
ATOM   4525  O  O     . LEU J  3 180 ? 46.710  44.969  139.508 1.00 17.96 ? 180  LEU B O     1 
ATOM   4526  C  CB    . LEU J  3 180 ? 46.292  47.384  141.285 1.00 13.00 ? 180  LEU B CB    1 
ATOM   4527  C  CG    . LEU J  3 180 ? 45.746  48.383  140.247 1.00 17.26 ? 180  LEU B CG    1 
ATOM   4528  C  CD1   . LEU J  3 180 ? 44.243  48.670  140.531 1.00 16.37 ? 180  LEU B CD1   1 
ATOM   4529  C  CD2   . LEU J  3 180 ? 46.590  49.670  140.263 1.00 18.58 ? 180  LEU B CD2   1 
ATOM   4530  N  N     . HIS J  3 181 ? 44.465  45.086  139.368 1.00 14.32 ? 181  HIS B N     1 
ATOM   4531  C  CA    . HIS J  3 181 ? 44.403  44.394  138.074 1.00 14.66 ? 181  HIS B CA    1 
ATOM   4532  C  C     . HIS J  3 181 ? 44.441  45.364  136.889 1.00 13.86 ? 181  HIS B C     1 
ATOM   4533  O  O     . HIS J  3 181 ? 45.116  45.105  135.884 1.00 15.37 ? 181  HIS B O     1 
ATOM   4534  C  CB    . HIS J  3 181 ? 43.112  43.554  137.971 1.00 14.69 ? 181  HIS B CB    1 
ATOM   4535  C  CG    . HIS J  3 181 ? 43.051  42.691  136.742 1.00 15.80 ? 181  HIS B CG    1 
ATOM   4536  N  ND1   . HIS J  3 181 ? 42.104  42.858  135.752 1.00 20.23 ? 181  HIS B ND1   1 
ATOM   4537  C  CD2   . HIS J  3 181 ? 43.823  41.646  136.354 1.00 13.30 ? 181  HIS B CD2   1 
ATOM   4538  C  CE1   . HIS J  3 181 ? 42.291  41.948  134.806 1.00 11.83 ? 181  HIS B CE1   1 
ATOM   4539  N  NE2   . HIS J  3 181 ? 43.326  41.202  135.148 1.00 21.07 ? 181  HIS B NE2   1 
ATOM   4540  N  N     . ALA J  3 182 ? 43.703  46.459  136.992 1.00 14.45 ? 182  ALA B N     1 
ATOM   4541  C  CA    . ALA J  3 182 ? 43.665  47.412  135.886 1.00 16.28 ? 182  ALA B CA    1 
ATOM   4542  C  C     . ALA J  3 182 ? 43.423  48.835  136.299 1.00 17.13 ? 182  ALA B C     1 
ATOM   4543  O  O     . ALA J  3 182 ? 42.739  49.123  137.296 1.00 15.02 ? 182  ALA B O     1 
ATOM   4544  C  CB    . ALA J  3 182 ? 42.595  46.984  134.886 1.00 15.15 ? 182  ALA B CB    1 
ATOM   4545  N  N     . SER J  3 183 ? 44.036  49.738  135.538 1.00 14.79 ? 183  SER B N     1 
ATOM   4546  C  CA    . SER J  3 183 ? 43.872  51.166  135.672 1.00 16.38 ? 183  SER B CA    1 
ATOM   4547  C  C     . SER J  3 183 ? 43.118  51.527  134.391 1.00 15.63 ? 183  SER B C     1 
ATOM   4548  O  O     . SER J  3 183 ? 43.618  51.295  133.274 1.00 16.56 ? 183  SER B O     1 
ATOM   4549  C  CB    . SER J  3 183 ? 45.228  51.883  135.675 1.00 16.69 ? 183  SER B CB    1 
ATOM   4550  O  OG    . SER J  3 183 ? 45.030  53.287  135.475 1.00 20.96 ? 183  SER B OG    1 
ATOM   4551  N  N     . ILE J  3 184 ? 41.915  52.077  134.551 1.00 14.61 ? 184  ILE B N     1 
ATOM   4552  C  CA    . ILE J  3 184 ? 41.115  52.453  133.392 1.00 14.97 ? 184  ILE B CA    1 
ATOM   4553  C  C     . ILE J  3 184 ? 40.869  53.946  133.436 1.00 16.01 ? 184  ILE B C     1 
ATOM   4554  O  O     . ILE J  3 184 ? 40.132  54.443  134.282 1.00 17.97 ? 184  ILE B O     1 
ATOM   4555  C  CB    . ILE J  3 184 ? 39.752  51.682  133.373 1.00 17.00 ? 184  ILE B CB    1 
ATOM   4556  C  CG1   . ILE J  3 184 ? 40.012  50.172  133.275 1.00 19.13 ? 184  ILE B CG1   1 
ATOM   4557  C  CG2   . ILE J  3 184 ? 38.892  52.111  132.160 1.00 18.29 ? 184  ILE B CG2   1 
ATOM   4558  C  CD1   . ILE J  3 184 ? 38.748  49.301  133.419 1.00 22.15 ? 184  ILE B CD1   1 
ATOM   4559  N  N     . SER J  3 185 ? 41.504  54.674  132.522 1.00 15.30 ? 185  SER B N     1 
ATOM   4560  C  CA    . SER J  3 185 ? 41.354  56.121  132.432 1.00 17.15 ? 185  SER B CA    1 
ATOM   4561  C  C     . SER J  3 185 ? 40.203  56.427  131.457 1.00 17.87 ? 185  SER B C     1 
ATOM   4562  O  O     . SER J  3 185 ? 40.102  55.787  130.414 1.00 18.26 ? 185  SER B O     1 
ATOM   4563  C  CB    . SER J  3 185 ? 42.659  56.709  131.905 1.00 21.65 ? 185  SER B CB    1 
ATOM   4564  O  OG    . SER J  3 185 ? 42.444  57.975  131.319 1.00 33.36 ? 185  SER B OG    1 
ATOM   4565  N  N     . CYS J  3 186 ? 39.338  57.376  131.817 1.00 14.37 ? 186  CYS B N     1 
ATOM   4566  C  CA    . CYS J  3 186 ? 38.221  57.753  130.954 1.00 15.65 ? 186  CYS B CA    1 
ATOM   4567  C  C     . CYS J  3 186 ? 38.363  59.206  130.512 1.00 16.18 ? 186  CYS B C     1 
ATOM   4568  O  O     . CYS J  3 186 ? 38.809  60.069  131.278 1.00 15.86 ? 186  CYS B O     1 
ATOM   4569  C  CB    . CYS J  3 186 ? 36.881  57.620  131.689 1.00 15.39 ? 186  CYS B CB    1 
ATOM   4570  S  SG    . CYS J  3 186 ? 36.488  55.917  132.166 1.00 20.21 ? 186  CYS B SG    1 
ATOM   4571  N  N     . LYS J  3 187 ? 37.970  59.466  129.265 1.00 15.22 ? 187  LYS B N     1 
ATOM   4572  C  CA    . LYS J  3 187 ? 37.970  60.817  128.705 1.00 17.14 ? 187  LYS B CA    1 
ATOM   4573  C  C     . LYS J  3 187 ? 36.747  60.935  127.793 1.00 16.52 ? 187  LYS B C     1 
ATOM   4574  O  O     . LYS J  3 187 ? 36.703  60.344  126.721 1.00 15.87 ? 187  LYS B O     1 
ATOM   4575  C  CB    . LYS J  3 187 ? 39.272  61.089  127.934 1.00 16.27 ? 187  LYS B CB    1 
ATOM   4576  C  CG    . LYS J  3 187 ? 40.494  61.048  128.859 1.00 16.12 ? 187  LYS B CG    1 
ATOM   4577  C  CD    . LYS J  3 187 ? 41.771  61.565  128.191 1.00 17.57 ? 187  LYS B CD    1 
ATOM   4578  C  CE    . LYS J  3 187 ? 42.940  61.554  129.148 1.00 16.49 ? 187  LYS B CE    1 
ATOM   4579  N  NZ    . LYS J  3 187 ? 42.658  62.465  130.310 1.00 18.98 ? 187  LYS B NZ    1 
ATOM   4580  N  N     . TRP J  3 188 ? 35.749  61.693  128.238 1.00 17.60 ? 188  TRP B N     1 
ATOM   4581  C  CA    . TRP J  3 188 ? 34.535  61.870  127.459 1.00 17.11 ? 188  TRP B CA    1 
ATOM   4582  C  C     . TRP J  3 188 ? 34.898  62.482  126.104 1.00 18.72 ? 188  TRP B C     1 
ATOM   4583  O  O     . TRP J  3 188 ? 34.470  61.979  125.067 1.00 18.11 ? 188  TRP B O     1 
ATOM   4584  C  CB    . TRP J  3 188 ? 33.538  62.716  128.265 1.00 18.31 ? 188  TRP B CB    1 
ATOM   4585  C  CG    . TRP J  3 188 ? 32.319  63.096  127.499 1.00 21.01 ? 188  TRP B CG    1 
ATOM   4586  C  CD1   . TRP J  3 188 ? 31.940  64.362  127.159 1.00 21.04 ? 188  TRP B CD1   1 
ATOM   4587  C  CD2   . TRP J  3 188 ? 31.346  62.213  126.925 1.00 23.21 ? 188  TRP B CD2   1 
ATOM   4588  N  NE1   . TRP J  3 188 ? 30.801  64.324  126.400 1.00 21.61 ? 188  TRP B NE1   1 
ATOM   4589  C  CE2   . TRP J  3 188 ? 30.413  63.021  126.235 1.00 23.71 ? 188  TRP B CE2   1 
ATOM   4590  C  CE3   . TRP J  3 188 ? 31.180  60.822  126.917 1.00 22.59 ? 188  TRP B CE3   1 
ATOM   4591  C  CZ2   . TRP J  3 188 ? 29.310  62.478  125.548 1.00 24.24 ? 188  TRP B CZ2   1 
ATOM   4592  C  CZ3   . TRP J  3 188 ? 30.078  60.280  126.227 1.00 26.50 ? 188  TRP B CZ3   1 
ATOM   4593  C  CH2   . TRP J  3 188 ? 29.167  61.109  125.551 1.00 25.29 ? 188  TRP B CH2   1 
ATOM   4594  N  N     . THR J  3 189 ? 35.693  63.551  126.113 1.00 16.08 ? 189  THR B N     1 
ATOM   4595  C  CA    . THR J  3 189 ? 36.185  64.142  124.861 1.00 19.56 ? 189  THR B CA    1 
ATOM   4596  C  C     . THR J  3 189 ? 37.665  64.389  125.129 1.00 18.23 ? 189  THR B C     1 
ATOM   4597  O  O     . THR J  3 189 ? 38.114  64.275  126.275 1.00 17.30 ? 189  THR B O     1 
ATOM   4598  C  CB    . THR J  3 189 ? 35.544  65.500  124.525 1.00 18.83 ? 189  THR B CB    1 
ATOM   4599  O  OG1   . THR J  3 189 ? 35.886  66.462  125.537 1.00 18.03 ? 189  THR B OG1   1 
ATOM   4600  C  CG2   . THR J  3 189 ? 34.024  65.345  124.421 1.00 23.72 ? 189  THR B CG2   1 
ATOM   4601  N  N     . ILE J  3 190 ? 38.397  64.758  124.087 1.00 19.33 ? 190  ILE B N     1 
ATOM   4602  C  CA    . ILE J  3 190 ? 39.831  65.000  124.199 1.00 16.29 ? 190  ILE B CA    1 
ATOM   4603  C  C     . ILE J  3 190 ? 40.301  66.325  123.573 1.00 21.77 ? 190  ILE B C     1 
ATOM   4604  O  O     . ILE J  3 190 ? 39.702  66.817  122.610 1.00 19.59 ? 190  ILE B O     1 
ATOM   4605  C  CB    . ILE J  3 190 ? 40.629  63.857  123.438 1.00 16.65 ? 190  ILE B CB    1 
ATOM   4606  C  CG1   . ILE J  3 190 ? 40.469  62.508  124.164 1.00 15.77 ? 190  ILE B CG1   1 
ATOM   4607  C  CG2   . ILE J  3 190 ? 42.103  64.240  123.272 1.00 16.95 ? 190  ILE B CG2   1 
ATOM   4608  C  CD1   . ILE J  3 190 ? 40.995  61.300  123.364 1.00 16.18 ? 190  ILE B CD1   1 
ATOM   4609  N  N     . ARG J  3 191 ? 41.340  66.910  124.168 1.00 18.94 ? 191  ARG B N     1 
ATOM   4610  C  CA    . ARG J  3 191 ? 42.063  68.031  123.569 1.00 16.00 ? 191  ARG B CA    1 
ATOM   4611  C  C     . ARG J  3 191 ? 43.475  67.469  123.751 1.00 18.05 ? 191  ARG B C     1 
ATOM   4612  O  O     . ARG J  3 191 ? 43.766  66.834  124.790 1.00 17.67 ? 191  ARG B O     1 
ATOM   4613  C  CB    . ARG J  3 191 ? 41.883  69.353  124.312 1.00 18.92 ? 191  ARG B CB    1 
ATOM   4614  C  CG    . ARG J  3 191 ? 40.475  69.962  124.134 1.00 18.98 ? 191  ARG B CG    1 
ATOM   4615  C  CD    . ARG J  3 191 ? 40.160  70.321  122.657 1.00 17.63 ? 191  ARG B CD    1 
ATOM   4616  N  NE    . ARG J  3 191 ? 38.846  70.991  122.603 1.00 17.25 ? 191  ARG B NE    1 
ATOM   4617  C  CZ    . ARG J  3 191 ? 37.675  70.366  122.499 1.00 21.73 ? 191  ARG B CZ    1 
ATOM   4618  N  NH1   . ARG J  3 191 ? 37.614  69.030  122.414 1.00 19.06 ? 191  ARG B NH1   1 
ATOM   4619  N  NH2   . ARG J  3 191 ? 36.540  71.080  122.531 1.00 19.81 ? 191  ARG B NH2   1 
ATOM   4620  N  N     . SER J  3 192 ? 44.338  67.675  122.764 1.00 18.58 ? 192  SER B N     1 
ATOM   4621  C  CA    . SER J  3 192 ? 45.682  67.096  122.815 1.00 19.97 ? 192  SER B CA    1 
ATOM   4622  C  C     . SER J  3 192 ? 46.548  67.474  124.009 1.00 18.32 ? 192  SER B C     1 
ATOM   4623  O  O     . SER J  3 192 ? 47.463  66.713  124.365 1.00 18.23 ? 192  SER B O     1 
ATOM   4624  C  CB    . SER J  3 192 ? 46.414  67.362  121.502 1.00 21.48 ? 192  SER B CB    1 
ATOM   4625  O  OG    . SER J  3 192 ? 46.558  68.743  121.294 1.00 20.54 ? 192  SER B OG    1 
ATOM   4626  N  N     . ASP J  3 193 ? 46.277  68.613  124.649 1.00 16.40 ? 193  ASP B N     1 
ATOM   4627  C  CA    . ASP J  3 193 ? 47.045  68.970  125.826 1.00 16.84 ? 193  ASP B CA    1 
ATOM   4628  C  C     . ASP J  3 193 ? 46.602  68.188  127.063 1.00 19.99 ? 193  ASP B C     1 
ATOM   4629  O  O     . ASP J  3 193 ? 47.440  67.554  127.758 1.00 20.37 ? 193  ASP B O     1 
ATOM   4630  C  CB    . ASP J  3 193 ? 46.982  70.477  126.104 1.00 17.56 ? 193  ASP B CB    1 
ATOM   4631  C  CG    . ASP J  3 193 ? 45.547  71.005  126.286 1.00 18.09 ? 193  ASP B CG    1 
ATOM   4632  O  OD1   . ASP J  3 193 ? 45.363  71.925  127.106 1.00 17.74 ? 193  ASP B OD1   1 
ATOM   4633  O  OD2   . ASP J  3 193 ? 44.626  70.504  125.618 1.00 18.75 ? 193  ASP B OD2   1 
ATOM   4634  N  N     . ARG J  3 194 ? 45.296  68.186  127.338 1.00 18.92 ? 194  ARG B N     1 
ATOM   4635  C  CA    . ARG J  3 194 ? 44.810  67.482  128.521 1.00 19.35 ? 194  ARG B CA    1 
ATOM   4636  C  C     . ARG J  3 194 ? 44.749  65.960  128.391 1.00 20.34 ? 194  ARG B C     1 
ATOM   4637  O  O     . ARG J  3 194 ? 44.517  65.254  129.368 1.00 24.42 ? 194  ARG B O     1 
ATOM   4638  C  CB    . ARG J  3 194 ? 43.450  68.050  128.972 1.00 21.93 ? 194  ARG B CB    1 
ATOM   4639  C  CG    . ARG J  3 194 ? 42.367  68.098  127.907 1.00 19.71 ? 194  ARG B CG    1 
ATOM   4640  C  CD    . ARG J  3 194 ? 41.080  68.745  128.493 1.00 20.80 ? 194  ARG B CD    1 
ATOM   4641  N  NE    . ARG J  3 194 ? 40.015  68.904  127.507 1.00 19.83 ? 194  ARG B NE    1 
ATOM   4642  C  CZ    . ARG J  3 194 ? 39.223  67.932  127.059 1.00 21.51 ? 194  ARG B CZ    1 
ATOM   4643  N  NH1   . ARG J  3 194 ? 39.351  66.675  127.507 1.00 18.19 ? 194  ARG B NH1   1 
ATOM   4644  N  NH2   . ARG J  3 194 ? 38.283  68.226  126.154 1.00 19.32 ? 194  ARG B NH2   1 
ATOM   4645  N  N     . ALA J  3 195 ? 44.965  65.435  127.192 1.00 16.31 ? 195  ALA B N     1 
ATOM   4646  C  CA    . ALA J  3 195 ? 44.964  63.995  127.024 1.00 19.01 ? 195  ALA B CA    1 
ATOM   4647  C  C     . ALA J  3 195 ? 46.235  63.386  127.620 1.00 16.67 ? 195  ALA B C     1 
ATOM   4648  O  O     . ALA J  3 195 ? 46.265  62.187  127.948 1.00 16.39 ? 195  ALA B O     1 
ATOM   4649  C  CB    . ALA J  3 195 ? 44.915  63.657  125.544 1.00 26.72 ? 195  ALA B CB    1 
ATOM   4650  N  N     . GLN J  3 196 ? 47.268  64.214  127.790 1.00 16.47 ? 196  GLN B N     1 
ATOM   4651  C  CA    . GLN J  3 196 ? 48.560  63.687  128.249 1.00 14.34 ? 196  GLN B CA    1 
ATOM   4652  C  C     . GLN J  3 196 ? 48.671  63.229  129.703 1.00 15.93 ? 196  GLN B C     1 
ATOM   4653  O  O     . GLN J  3 196 ? 49.641  62.557  130.061 1.00 14.83 ? 196  GLN B O     1 
ATOM   4654  C  CB    . GLN J  3 196 ? 49.672  64.693  127.924 1.00 16.01 ? 196  GLN B CB    1 
ATOM   4655  C  CG    . GLN J  3 196 ? 49.687  65.162  126.453 1.00 17.30 ? 196  GLN B CG    1 
ATOM   4656  C  CD    . GLN J  3 196 ? 49.647  64.017  125.463 1.00 19.41 ? 196  GLN B CD    1 
ATOM   4657  O  OE1   . GLN J  3 196 ? 50.337  62.992  125.627 1.00 20.00 ? 196  GLN B OE1   1 
ATOM   4658  N  NE2   . GLN J  3 196 ? 48.849  64.182  124.406 1.00 19.01 ? 196  GLN B NE2   1 
ATOM   4659  N  N     . ASN J  3 197 ? 47.711  63.592  130.543 1.00 16.62 ? 197  ASN B N     1 
ATOM   4660  C  CA    . ASN J  3 197 ? 47.798  63.123  131.928 1.00 15.97 ? 197  ASN B CA    1 
ATOM   4661  C  C     . ASN J  3 197 ? 47.634  61.599  132.001 1.00 17.66 ? 197  ASN B C     1 
ATOM   4662  O  O     . ASN J  3 197 ? 48.035  60.982  132.991 1.00 16.48 ? 197  ASN B O     1 
ATOM   4663  C  CB    . ASN J  3 197 ? 46.795  63.872  132.829 1.00 15.57 ? 197  ASN B CB    1 
ATOM   4664  C  CG    . ASN J  3 197 ? 45.329  63.596  132.476 1.00 17.73 ? 197  ASN B CG    1 
ATOM   4665  O  OD1   . ASN J  3 197 ? 44.994  63.117  131.388 1.00 16.61 ? 197  ASN B OD1   1 
ATOM   4666  N  ND2   . ASN J  3 197 ? 44.448  63.941  133.405 1.00 16.70 ? 197  ASN B ND2   1 
ATOM   4667  N  N     . ALA J  3 198 ? 47.056  60.992  130.955 1.00 14.36 ? 198  ALA B N     1 
ATOM   4668  C  CA    . ALA J  3 198 ? 46.931  59.537  130.898 1.00 14.90 ? 198  ALA B CA    1 
ATOM   4669  C  C     . ALA J  3 198 ? 48.348  58.933  130.784 1.00 14.86 ? 198  ALA B C     1 
ATOM   4670  O  O     . ALA J  3 198 ? 48.623  57.861  131.345 1.00 15.30 ? 198  ALA B O     1 
ATOM   4671  C  CB    . ALA J  3 198 ? 46.091  59.101  129.700 1.00 18.41 ? 198  ALA B CB    1 
ATOM   4672  N  N     . ARG J  3 199 ? 49.254  59.613  130.077 1.00 14.19 ? 199  ARG B N     1 
ATOM   4673  C  CA    . ARG J  3 199 ? 50.615  59.104  129.936 1.00 15.36 ? 199  ARG B CA    1 
ATOM   4674  C  C     . ARG J  3 199 ? 51.417  59.260  131.225 1.00 15.29 ? 199  ARG B C     1 
ATOM   4675  O  O     . ARG J  3 199 ? 52.140  58.336  131.616 1.00 16.71 ? 199  ARG B O     1 
ATOM   4676  C  CB    . ARG J  3 199 ? 51.360  59.803  128.783 1.00 20.35 ? 199  ARG B CB    1 
ATOM   4677  C  CG    . ARG J  3 199 ? 50.756  59.579  127.415 1.00 19.87 ? 199  ARG B CG    1 
ATOM   4678  C  CD    . ARG J  3 199 ? 51.665  60.210  126.330 1.00 19.71 ? 199  ARG B CD    1 
ATOM   4679  N  NE    . ARG J  3 199 ? 50.983  60.340  125.037 1.00 21.40 ? 199  ARG B NE    1 
ATOM   4680  C  CZ    . ARG J  3 199 ? 50.959  59.413  124.095 1.00 21.61 ? 199  ARG B CZ    1 
ATOM   4681  N  NH1   . ARG J  3 199 ? 51.584  58.251  124.274 1.00 21.05 ? 199  ARG B NH1   1 
ATOM   4682  N  NH2   . ARG J  3 199 ? 50.318  59.657  122.961 1.00 22.79 ? 199  ARG B NH2   1 
ATOM   4683  N  N     . SER J  3 200 ? 51.293  60.408  131.891 1.00 14.12 ? 200  SER B N     1 
ATOM   4684  C  CA    . SER J  3 200 ? 52.048  60.613  133.123 1.00 17.13 ? 200  SER B CA    1 
ATOM   4685  C  C     . SER J  3 200 ? 51.541  59.647  134.201 1.00 16.04 ? 200  SER B C     1 
ATOM   4686  O  O     . SER J  3 200 ? 52.341  59.122  134.999 1.00 17.54 ? 200  SER B O     1 
ATOM   4687  C  CB    . SER J  3 200 ? 51.958  62.082  133.600 1.00 19.24 ? 200  SER B CB    1 
ATOM   4688  O  OG    . SER J  3 200 ? 50.614  62.494  133.778 1.00 19.71 ? 200  SER B OG    1 
ATOM   4689  N  N     . GLU J  3 201 ? 50.239  59.401  134.239 1.00 15.43 ? 201  GLU B N     1 
ATOM   4690  C  CA    . GLU J  3 201 ? 49.712  58.480  135.253 1.00 15.36 ? 201  GLU B CA    1 
ATOM   4691  C  C     . GLU J  3 201 ? 50.179  57.063  134.934 1.00 16.89 ? 201  GLU B C     1 
ATOM   4692  O  O     . GLU J  3 201 ? 50.559  56.306  135.839 1.00 16.98 ? 201  GLU B O     1 
ATOM   4693  C  CB    . GLU J  3 201 ? 48.176  58.597  135.338 1.00 18.85 ? 201  GLU B CB    1 
ATOM   4694  C  CG    . GLU J  3 201 ? 47.807  59.931  136.036 1.00 23.63 ? 201  GLU B CG    1 
ATOM   4695  C  CD    . GLU J  3 201 ? 46.314  60.177  136.222 1.00 32.59 ? 201  GLU B CD    1 
ATOM   4696  O  OE1   . GLU J  3 201 ? 45.584  59.201  136.540 1.00 28.69 ? 201  GLU B OE1   1 
ATOM   4697  O  OE2   . GLU J  3 201 ? 45.882  61.355  136.067 1.00 29.42 ? 201  GLU B OE2   1 
ATOM   4698  N  N     . GLY J  3 202 ? 50.173  56.702  133.651 1.00 16.06 ? 202  GLY B N     1 
ATOM   4699  C  CA    . GLY J  3 202 ? 50.643  55.388  133.253 1.00 17.86 ? 202  GLY B CA    1 
ATOM   4700  C  C     . GLY J  3 202 ? 52.108  55.182  133.615 1.00 17.69 ? 202  GLY B C     1 
ATOM   4701  O  O     . GLY J  3 202 ? 52.488  54.101  134.085 1.00 18.10 ? 202  GLY B O     1 
ATOM   4702  N  N     . LEU J  3 203 ? 52.933  56.201  133.394 1.00 15.91 ? 203  LEU B N     1 
ATOM   4703  C  CA    . LEU J  3 203 ? 54.361  56.110  133.710 1.00 16.75 ? 203  LEU B CA    1 
ATOM   4704  C  C     . LEU J  3 203 ? 54.566  55.933  135.215 1.00 15.96 ? 203  LEU B C     1 
ATOM   4705  O  O     . LEU J  3 203 ? 55.459  55.182  135.630 1.00 15.28 ? 203  LEU B O     1 
ATOM   4706  C  CB    . LEU J  3 203 ? 55.078  57.367  133.236 1.00 19.01 ? 203  LEU B CB    1 
ATOM   4707  C  CG    . LEU J  3 203 ? 56.598  57.363  133.309 1.00 27.58 ? 203  LEU B CG    1 
ATOM   4708  C  CD1   . LEU J  3 203 ? 57.149  56.246  132.415 1.00 31.59 ? 203  LEU B CD1   1 
ATOM   4709  C  CD2   . LEU J  3 203 ? 57.101  58.726  132.864 1.00 33.13 ? 203  LEU B CD2   1 
ATOM   4710  N  N     . ASN J  3 204 ? 53.762  56.613  136.029 1.00 15.77 ? 204  ASN B N     1 
ATOM   4711  C  CA    . ASN J  3 204 ? 53.907  56.439  137.476 1.00 16.88 ? 204  ASN B CA    1 
ATOM   4712  C  C     . ASN J  3 204 ? 53.598  54.997  137.881 1.00 16.64 ? 204  ASN B C     1 
ATOM   4713  O  O     . ASN J  3 204 ? 54.248  54.429  138.773 1.00 17.27 ? 204  ASN B O     1 
ATOM   4714  C  CB    . ASN J  3 204 ? 53.029  57.428  138.246 1.00 20.68 ? 204  ASN B CB    1 
ATOM   4715  C  CG    . ASN J  3 204 ? 53.682  58.813  138.361 1.00 31.07 ? 204  ASN B CG    1 
ATOM   4716  O  OD1   . ASN J  3 204 ? 54.910  58.924  138.486 1.00 34.07 ? 204  ASN B OD1   1 
ATOM   4717  N  ND2   . ASN J  3 204 ? 52.868  59.865  138.336 1.00 32.25 ? 204  ASN B ND2   1 
ATOM   4718  N  N     . LEU J  3 205 ? 52.629  54.371  137.215 1.00 16.32 ? 205  LEU B N     1 
ATOM   4719  C  CA    . LEU J  3 205 ? 52.299  52.970  137.520 1.00 16.32 ? 205  LEU B CA    1 
ATOM   4720  C  C     . LEU J  3 205 ? 53.447  52.053  137.072 1.00 14.94 ? 205  LEU B C     1 
ATOM   4721  O  O     . LEU J  3 205 ? 53.785  51.083  137.737 1.00 15.35 ? 205  LEU B O     1 
ATOM   4722  C  CB    . LEU J  3 205 ? 51.007  52.541  136.815 1.00 16.95 ? 205  LEU B CB    1 
ATOM   4723  C  CG    . LEU J  3 205 ? 49.766  53.257  137.314 1.00 19.95 ? 205  LEU B CG    1 
ATOM   4724  C  CD1   . LEU J  3 205 ? 48.590  52.912  136.399 1.00 20.97 ? 205  LEU B CD1   1 
ATOM   4725  C  CD2   . LEU J  3 205 ? 49.493  52.850  138.751 1.00 22.27 ? 205  LEU B CD2   1 
ATOM   4726  N  N     . VAL J  3 206 ? 54.064  52.373  135.940 1.00 13.43 ? 206  VAL B N     1 
ATOM   4727  C  CA    . VAL J  3 206 ? 55.178  51.563  135.464 1.00 13.19 ? 206  VAL B CA    1 
ATOM   4728  C  C     . VAL J  3 206 ? 56.388  51.690  136.396 1.00 14.45 ? 206  VAL B C     1 
ATOM   4729  O  O     . VAL J  3 206 ? 56.970  50.687  136.834 1.00 14.36 ? 206  VAL B O     1 
ATOM   4730  C  CB    . VAL J  3 206 ? 55.639  52.030  134.056 1.00 14.60 ? 206  VAL B CB    1 
ATOM   4731  C  CG1   . VAL J  3 206 ? 56.960  51.337  133.676 1.00 18.17 ? 206  VAL B CG1   1 
ATOM   4732  C  CG2   . VAL J  3 206 ? 54.564  51.759  133.031 1.00 17.12 ? 206  VAL B CG2   1 
ATOM   4733  N  N     . ARG J  3 207 ? 56.726  52.926  136.736 1.00 15.18 ? 207  ARG B N     1 
ATOM   4734  C  CA    . ARG J  3 207 ? 57.932  53.189  137.517 1.00 17.93 ? 207  ARG B CA    1 
ATOM   4735  C  C     . ARG J  3 207 ? 57.946  52.722  138.957 1.00 16.43 ? 207  ARG B C     1 
ATOM   4736  O  O     . ARG J  3 207 ? 58.993  52.368  139.474 1.00 17.78 ? 207  ARG B O     1 
ATOM   4737  C  CB    . ARG J  3 207 ? 58.264  54.693  137.464 1.00 20.32 ? 207  ARG B CB    1 
ATOM   4738  C  CG    . ARG J  3 207 ? 58.707  55.140  136.069 1.00 28.90 ? 207  ARG B CG    1 
ATOM   4739  C  CD    . ARG J  3 207 ? 58.986  56.648  135.938 1.00 40.22 ? 207  ARG B CD    1 
ATOM   4740  N  NE    . ARG J  3 207 ? 59.496  56.935  134.595 1.00 47.68 ? 207  ARG B NE    1 
ATOM   4741  C  CZ    . ARG J  3 207 ? 59.728  58.149  134.103 1.00 53.29 ? 207  ARG B CZ    1 
ATOM   4742  N  NH1   . ARG J  3 207 ? 59.497  59.230  134.841 1.00 56.83 ? 207  ARG B NH1   1 
ATOM   4743  N  NH2   . ARG J  3 207 ? 60.183  58.282  132.859 1.00 52.19 ? 207  ARG B NH2   1 
ATOM   4744  N  N     . ASN J  3 208 ? 56.778  52.662  139.580 1.00 14.72 ? 208  ASN B N     1 
ATOM   4745  C  CA    . ASN J  3 208 ? 56.705  52.337  141.007 1.00 17.60 ? 208  ASN B CA    1 
ATOM   4746  C  C     . ASN J  3 208 ? 56.186  50.978  141.399 1.00 18.02 ? 208  ASN B C     1 
ATOM   4747  O  O     . ASN J  3 208 ? 56.015  50.672  142.597 1.00 21.00 ? 208  ASN B O     1 
ATOM   4748  C  CB    . ASN J  3 208 ? 55.856  53.417  141.678 1.00 17.70 ? 208  ASN B CB    1 
ATOM   4749  C  CG    . ASN J  3 208 ? 56.539  54.775  141.657 1.00 21.50 ? 208  ASN B CG    1 
ATOM   4750  O  OD1   . ASN J  3 208 ? 57.551  54.967  142.320 1.00 29.58 ? 208  ASN B OD1   1 
ATOM   4751  N  ND2   . ASN J  3 208 ? 56.003  55.711  140.889 1.00 24.92 ? 208  ASN B ND2   1 
ATOM   4752  N  N     . ARG J  3 209 ? 55.972  50.116  140.421 1.00 14.22 ? 209  ARG B N     1 
ATOM   4753  C  CA    . ARG J  3 209 ? 55.388  48.834  140.746 1.00 14.41 ? 209  ARG B CA    1 
ATOM   4754  C  C     . ARG J  3 209 ? 56.325  47.809  141.377 1.00 16.13 ? 209  ARG B C     1 
ATOM   4755  O  O     . ARG J  3 209 ? 57.545  47.806  141.146 1.00 16.43 ? 209  ARG B O     1 
ATOM   4756  C  CB    . ARG J  3 209 ? 54.826  48.198  139.467 1.00 17.37 ? 209  ARG B CB    1 
ATOM   4757  C  CG    . ARG J  3 209 ? 55.927  47.499  138.635 1.00 17.00 ? 209  ARG B CG    1 
ATOM   4758  C  CD    . ARG J  3 209 ? 55.389  47.007  137.285 1.00 16.61 ? 209  ARG B CD    1 
ATOM   4759  N  NE    . ARG J  3 209 ? 56.396  46.212  136.575 1.00 15.05 ? 209  ARG B NE    1 
ATOM   4760  C  CZ    . ARG J  3 209 ? 57.378  46.696  135.813 1.00 13.74 ? 209  ARG B CZ    1 
ATOM   4761  N  NH1   . ARG J  3 209 ? 57.496  48.006  135.623 1.00 14.46 ? 209  ARG B NH1   1 
ATOM   4762  N  NH2   . ARG J  3 209 ? 58.270  45.857  135.282 1.00 14.48 ? 209  ARG B NH2   1 
ATOM   4763  N  N     . LYS J  3 210 ? 55.724  46.955  142.201 1.00 16.49 ? 210  LYS B N     1 
ATOM   4764  C  CA    . LYS J  3 210 ? 56.410  45.790  142.742 1.00 16.48 ? 210  LYS B CA    1 
ATOM   4765  C  C     . LYS J  3 210 ? 55.445  44.705  142.298 1.00 19.11 ? 210  LYS B C     1 
ATOM   4766  O  O     . LYS J  3 210 ? 54.307  44.658  142.751 1.00 24.61 ? 210  LYS B O     1 
ATOM   4767  C  CB    . LYS J  3 210 ? 56.527  45.855  144.263 1.00 16.66 ? 210  LYS B CB    1 
ATOM   4768  C  CG    . LYS J  3 210 ? 57.570  46.881  144.684 1.00 16.49 ? 210  LYS B CG    1 
ATOM   4769  C  CD    . LYS J  3 210 ? 57.827  46.783  146.173 1.00 22.72 ? 210  LYS B CD    1 
ATOM   4770  C  CE    . LYS J  3 210 ? 58.672  47.953  146.647 1.00 22.58 ? 210  LYS B CE    1 
ATOM   4771  N  NZ    . LYS J  3 210 ? 58.905  47.808  148.135 1.00 26.72 ? 210  LYS B NZ    1 
ATOM   4772  N  N     . GLY J  3 211 ? 55.867  43.842  141.391 1.00 17.63 ? 211  GLY B N     1 
ATOM   4773  C  CA    . GLY J  3 211 ? 54.951  42.837  140.894 1.00 16.08 ? 211  GLY B CA    1 
ATOM   4774  C  C     . GLY J  3 211 ? 54.578  43.137  139.441 1.00 17.89 ? 211  GLY B C     1 
ATOM   4775  O  O     . GLY J  3 211 ? 55.169  44.044  138.839 1.00 16.53 ? 211  GLY B O     1 
ATOM   4776  N  N     . ARG J  3 212 ? 53.622  42.390  138.886 1.00 16.69 ? 212  ARG B N     1 
ATOM   4777  C  CA    . ARG J  3 212 ? 53.227  42.583  137.481 1.00 14.95 ? 212  ARG B CA    1 
ATOM   4778  C  C     . ARG J  3 212 ? 52.459  43.881  137.300 1.00 16.41 ? 212  ARG B C     1 
ATOM   4779  O  O     . ARG J  3 212 ? 51.579  44.235  138.087 1.00 18.25 ? 212  ARG B O     1 
ATOM   4780  C  CB    . ARG J  3 212 ? 52.366  41.422  136.957 1.00 15.78 ? 212  ARG B CB    1 
ATOM   4781  C  CG    . ARG J  3 212 ? 52.136  41.521  135.431 1.00 15.19 ? 212  ARG B CG    1 
ATOM   4782  C  CD    . ARG J  3 212 ? 51.328  40.357  134.833 1.00 17.84 ? 212  ARG B CD    1 
ATOM   4783  N  NE    . ARG J  3 212 ? 51.190  40.542  133.379 1.00 16.74 ? 212  ARG B NE    1 
ATOM   4784  C  CZ    . ARG J  3 212 ? 50.462  39.773  132.573 1.00 21.20 ? 212  ARG B CZ    1 
ATOM   4785  N  NH1   . ARG J  3 212 ? 49.776  38.738  133.051 1.00 21.44 ? 212  ARG B NH1   1 
ATOM   4786  N  NH2   . ARG J  3 212 ? 50.430  40.047  131.269 1.00 20.20 ? 212  ARG B NH2   1 
ATOM   4787  N  N     . LEU J  3 213 ? 52.804  44.602  136.246 1.00 13.86 ? 213  LEU B N     1 
ATOM   4788  C  CA    . LEU J  3 213 ? 52.119  45.847  135.960 1.00 13.53 ? 213  LEU B CA    1 
ATOM   4789  C  C     . LEU J  3 213 ? 50.652  45.579  135.661 1.00 14.32 ? 213  LEU B C     1 
ATOM   4790  O  O     . LEU J  3 213 ? 50.316  44.632  134.955 1.00 14.26 ? 213  LEU B O     1 
ATOM   4791  C  CB    . LEU J  3 213 ? 52.741  46.494  134.722 1.00 11.67 ? 213  LEU B CB    1 
ATOM   4792  C  CG    . LEU J  3 213 ? 52.275  47.902  134.329 1.00 11.91 ? 213  LEU B CG    1 
ATOM   4793  C  CD1   . LEU J  3 213 ? 52.831  48.895  135.327 1.00 12.88 ? 213  LEU B CD1   1 
ATOM   4794  C  CD2   . LEU J  3 213 ? 52.766  48.252  132.927 1.00 15.20 ? 213  LEU B CD2   1 
ATOM   4795  N  N     . PRO J  3 214 ? 49.751  46.411  136.197 1.00 13.39 ? 214  PRO B N     1 
ATOM   4796  C  CA    . PRO J  3 214 ? 48.316  46.215  135.908 1.00 14.32 ? 214  PRO B CA    1 
ATOM   4797  C  C     . PRO J  3 214 ? 48.050  46.558  134.424 1.00 15.71 ? 214  PRO B C     1 
ATOM   4798  O  O     . PRO J  3 214 ? 48.912  47.122  133.736 1.00 14.98 ? 214  PRO B O     1 
ATOM   4799  C  CB    . PRO J  3 214 ? 47.627  47.312  136.720 1.00 20.95 ? 214  PRO B CB    1 
ATOM   4800  C  CG    . PRO J  3 214 ? 48.643  47.698  137.795 1.00 24.69 ? 214  PRO B CG    1 
ATOM   4801  C  CD    . PRO J  3 214 ? 49.994  47.531  137.127 1.00 14.48 ? 214  PRO B CD    1 
ATOM   4802  N  N     . HIS J  3 215 ? 46.856  46.213  133.952 1.00 14.78 ? 215  HIS B N     1 
ATOM   4803  C  CA    . HIS J  3 215 ? 46.425  46.676  132.632 1.00 14.47 ? 215  HIS B CA    1 
ATOM   4804  C  C     . HIS J  3 215 ? 46.379  48.214  132.775 1.00 14.29 ? 215  HIS B C     1 
ATOM   4805  O  O     . HIS J  3 215 ? 45.998  48.722  133.837 1.00 15.40 ? 215  HIS B O     1 
ATOM   4806  C  CB    . HIS J  3 215 ? 44.981  46.227  132.358 1.00 13.27 ? 215  HIS B CB    1 
ATOM   4807  C  CG    . HIS J  3 215 ? 44.865  44.796  131.946 1.00 15.27 ? 215  HIS B CG    1 
ATOM   4808  N  ND1   . HIS J  3 215 ? 44.635  43.766  132.838 1.00 17.55 ? 215  HIS B ND1   1 
ATOM   4809  C  CD2   . HIS J  3 215 ? 44.992  44.223  130.733 1.00 12.27 ? 215  HIS B CD2   1 
ATOM   4810  C  CE1   . HIS J  3 215 ? 44.619  42.620  132.180 1.00 15.83 ? 215  HIS B CE1   1 
ATOM   4811  N  NE2   . HIS J  3 215 ? 44.831  42.872  130.900 1.00 20.53 ? 215  HIS B NE2   1 
ATOM   4812  N  N     . ILE J  3 216 ? 46.750  48.949  131.722 1.00 14.31 ? 216  ILE B N     1 
ATOM   4813  C  CA    . ILE J  3 216 ? 46.691  50.415  131.736 1.00 12.69 ? 216  ILE B CA    1 
ATOM   4814  C  C     . ILE J  3 216 ? 46.025  50.777  130.416 1.00 15.01 ? 216  ILE B C     1 
ATOM   4815  O  O     . ILE J  3 216 ? 46.659  50.677  129.364 1.00 14.20 ? 216  ILE B O     1 
ATOM   4816  C  CB    . ILE J  3 216 ? 48.090  51.098  131.783 1.00 14.37 ? 216  ILE B CB    1 
ATOM   4817  C  CG1   . ILE J  3 216 ? 48.848  50.697  133.071 1.00 15.92 ? 216  ILE B CG1   1 
ATOM   4818  C  CG2   . ILE J  3 216 ? 47.934  52.607  131.797 1.00 15.68 ? 216  ILE B CG2   1 
ATOM   4819  C  CD1   . ILE J  3 216 ? 50.285  51.257  133.099 1.00 15.63 ? 216  ILE B CD1   1 
ATOM   4820  N  N     . VAL J  3 217 ? 44.765  51.201  130.483 1.00 13.53 ? 217  VAL B N     1 
ATOM   4821  C  CA    . VAL J  3 217 ? 44.027  51.514  129.264 1.00 15.08 ? 217  VAL B CA    1 
ATOM   4822  C  C     . VAL J  3 217 ? 43.258  52.819  129.365 1.00 14.85 ? 217  VAL B C     1 
ATOM   4823  O  O     . VAL J  3 217 ? 43.112  53.390  130.444 1.00 14.96 ? 217  VAL B O     1 
ATOM   4824  C  CB    . VAL J  3 217 ? 43.011  50.390  128.936 1.00 15.14 ? 217  VAL B CB    1 
ATOM   4825  C  CG1   . VAL J  3 217 ? 43.744  49.049  128.736 1.00 18.02 ? 217  VAL B CG1   1 
ATOM   4826  C  CG2   . VAL J  3 217 ? 41.975  50.286  130.053 1.00 15.89 ? 217  VAL B CG2   1 
ATOM   4827  N  N     . VAL J  3 218 ? 42.812  53.309  128.213 1.00 14.20 ? 218  VAL B N     1 
ATOM   4828  C  CA    . VAL J  3 218 ? 42.027  54.532  128.153 1.00 14.36 ? 218  VAL B CA    1 
ATOM   4829  C  C     . VAL J  3 218 ? 40.756  54.220  127.375 1.00 14.95 ? 218  VAL B C     1 
ATOM   4830  O  O     . VAL J  3 218 ? 40.805  53.512  126.374 1.00 17.06 ? 218  VAL B O     1 
ATOM   4831  C  CB    . VAL J  3 218 ? 42.780  55.655  127.409 1.00 16.23 ? 218  VAL B CB    1 
ATOM   4832  C  CG1   . VAL J  3 218 ? 41.897  56.914  127.311 1.00 17.82 ? 218  VAL B CG1   1 
ATOM   4833  C  CG2   . VAL J  3 218 ? 44.077  55.992  128.175 1.00 15.17 ? 218  VAL B CG2   1 
ATOM   4834  N  N     . VAL J  3 219 ? 39.639  54.760  127.851 1.00 16.73 ? 219  VAL B N     1 
ATOM   4835  C  CA    . VAL J  3 219 ? 38.346  54.602  127.174 1.00 18.07 ? 219  VAL B CA    1 
ATOM   4836  C  C     . VAL J  3 219 ? 37.899  56.025  126.849 1.00 16.67 ? 219  VAL B C     1 
ATOM   4837  O  O     . VAL J  3 219 ? 37.926  56.890  127.706 1.00 16.90 ? 219  VAL B O     1 
ATOM   4838  C  CB    . VAL J  3 219 ? 37.298  53.939  128.100 1.00 19.33 ? 219  VAL B CB    1 
ATOM   4839  C  CG1   . VAL J  3 219 ? 35.926  53.844  127.376 1.00 18.96 ? 219  VAL B CG1   1 
ATOM   4840  C  CG2   . VAL J  3 219 ? 37.800  52.538  128.527 1.00 18.18 ? 219  VAL B CG2   1 
ATOM   4841  N  N     . THR J  3 220 ? 37.492  56.281  125.614 1.00 17.40 ? 220  THR B N     1 
ATOM   4842  C  CA    . THR J  3 220 ? 37.087  57.636  125.261 1.00 18.73 ? 220  THR B CA    1 
ATOM   4843  C  C     . THR J  3 220 ? 35.883  57.677  124.314 1.00 18.80 ? 220  THR B C     1 
ATOM   4844  O  O     . THR J  3 220 ? 35.610  56.720  123.603 1.00 19.77 ? 220  THR B O     1 
ATOM   4845  C  CB    . THR J  3 220 ? 38.263  58.385  124.571 1.00 18.97 ? 220  THR B CB    1 
ATOM   4846  O  OG1   . THR J  3 220 ? 37.926  59.769  124.385 1.00 19.69 ? 220  THR B OG1   1 
ATOM   4847  C  CG2   . THR J  3 220 ? 38.588  57.753  123.200 1.00 18.44 ? 220  THR B CG2   1 
ATOM   4848  N  N     . ALA J  3 221 ? 35.190  58.808  124.322 1.00 19.93 ? 221  ALA B N     1 
ATOM   4849  C  CA    . ALA J  3 221 ? 34.052  59.011  123.433 1.00 19.81 ? 221  ALA B CA    1 
ATOM   4850  C  C     . ALA J  3 221 ? 34.402  60.105  122.410 1.00 21.16 ? 221  ALA B C     1 
ATOM   4851  O  O     . ALA J  3 221 ? 33.532  60.564  121.653 1.00 21.29 ? 221  ALA B O     1 
ATOM   4852  C  CB    . ALA J  3 221 ? 32.806  59.396  124.243 1.00 21.20 ? 221  ALA B CB    1 
ATOM   4853  N  N     . GLU J  3 222 ? 35.676  60.512  122.372 1.00 18.71 ? 222  GLU B N     1 
ATOM   4854  C  CA    . GLU J  3 222 ? 36.128  61.546  121.430 1.00 19.13 ? 222  GLU B CA    1 
ATOM   4855  C  C     . GLU J  3 222 ? 35.783  61.118  120.007 1.00 20.40 ? 222  GLU B C     1 
ATOM   4856  O  O     . GLU J  3 222 ? 36.111  60.023  119.578 1.00 20.95 ? 222  GLU B O     1 
ATOM   4857  C  CB    . GLU J  3 222 ? 37.649  61.773  121.574 1.00 20.36 ? 222  GLU B CB    1 
ATOM   4858  C  CG    . GLU J  3 222 ? 38.258  62.634  120.464 1.00 19.58 ? 222  GLU B CG    1 
ATOM   4859  C  CD    . GLU J  3 222 ? 37.577  63.997  120.339 1.00 19.58 ? 222  GLU B CD    1 
ATOM   4860  O  OE1   . GLU J  3 222 ? 37.417  64.480  119.196 1.00 19.93 ? 222  GLU B OE1   1 
ATOM   4861  O  OE2   . GLU J  3 222 ? 37.212  64.605  121.368 1.00 17.80 ? 222  GLU B OE2   1 
ATOM   4862  N  N     . PRO J  3 223 ? 35.127  61.997  119.232 1.00 20.67 ? 223  PRO B N     1 
ATOM   4863  C  CA    . PRO J  3 223 ? 34.793  61.551  117.878 1.00 22.26 ? 223  PRO B CA    1 
ATOM   4864  C  C     . PRO J  3 223 ? 35.868  61.574  116.800 1.00 20.48 ? 223  PRO B C     1 
ATOM   4865  O  O     . PRO J  3 223 ? 35.832  60.756  115.880 1.00 23.85 ? 223  PRO B O     1 
ATOM   4866  C  CB    . PRO J  3 223 ? 33.576  62.430  117.515 1.00 20.70 ? 223  PRO B CB    1 
ATOM   4867  C  CG    . PRO J  3 223 ? 33.845  63.697  118.235 1.00 21.01 ? 223  PRO B CG    1 
ATOM   4868  C  CD    . PRO J  3 223 ? 34.346  63.185  119.621 1.00 18.76 ? 223  PRO B CD    1 
ATOM   4869  N  N     . THR J  3 224 ? 36.828  62.490  116.900 1.00 19.95 ? 224  THR B N     1 
ATOM   4870  C  CA    . THR J  3 224 ? 37.834  62.599  115.863 1.00 22.69 ? 224  THR B CA    1 
ATOM   4871  C  C     . THR J  3 224 ? 39.072  61.727  115.986 1.00 26.45 ? 224  THR B C     1 
ATOM   4872  O  O     . THR J  3 224 ? 39.704  61.663  117.044 1.00 21.95 ? 224  THR B O     1 
ATOM   4873  C  CB    . THR J  3 224 ? 38.317  64.048  115.702 1.00 22.68 ? 224  THR B CB    1 
ATOM   4874  O  OG1   . THR J  3 224 ? 39.006  64.473  116.885 1.00 20.21 ? 224  THR B OG1   1 
ATOM   4875  C  CG2   . THR J  3 224 ? 37.122  64.985  115.492 1.00 21.09 ? 224  THR B CG2   1 
ATOM   4876  N  N     . PRO J  3 225 ? 39.429  61.031  114.897 1.00 24.46 ? 225  PRO B N     1 
ATOM   4877  C  CA    . PRO J  3 225 ? 40.631  60.191  114.960 1.00 25.26 ? 225  PRO B CA    1 
ATOM   4878  C  C     . PRO J  3 225 ? 41.889  61.020  115.321 1.00 24.50 ? 225  PRO B C     1 
ATOM   4879  O  O     . PRO J  3 225 ? 42.796  60.530  116.011 1.00 21.54 ? 225  PRO B O     1 
ATOM   4880  C  CB    . PRO J  3 225 ? 40.694  59.589  113.553 1.00 26.49 ? 225  PRO B CB    1 
ATOM   4881  C  CG    . PRO J  3 225 ? 39.241  59.409  113.213 1.00 24.80 ? 225  PRO B CG    1 
ATOM   4882  C  CD    . PRO J  3 225 ? 38.641  60.736  113.680 1.00 25.25 ? 225  PRO B CD    1 
ATOM   4883  N  N     . SER J  3 226 ? 41.935  62.282  114.887 1.00 21.70 ? 226  SER B N     1 
ATOM   4884  C  CA    . SER J  3 226 ? 43.085  63.138  115.157 1.00 20.16 ? 226  SER B CA    1 
ATOM   4885  C  C     . SER J  3 226 ? 43.242  63.326  116.679 1.00 21.27 ? 226  SER B C     1 
ATOM   4886  O  O     . SER J  3 226 ? 44.336  63.158  117.217 1.00 24.96 ? 226  SER B O     1 
ATOM   4887  C  CB    . SER J  3 226 ? 42.920  64.501  114.468 1.00 23.21 ? 226  SER B CB    1 
ATOM   4888  O  OG    . SER J  3 226 ? 41.801  65.193  114.990 1.00 26.38 ? 226  SER B OG    1 
ATOM   4889  N  N     . ARG J  3 227 ? 42.164  63.669  117.368 1.00 19.77 ? 227  ARG B N     1 
ATOM   4890  C  CA    . ARG J  3 227 ? 42.281  63.852  118.820 1.00 19.72 ? 227  ARG B CA    1 
ATOM   4891  C  C     . ARG J  3 227 ? 42.539  62.528  119.528 1.00 20.05 ? 227  ARG B C     1 
ATOM   4892  O  O     . ARG J  3 227 ? 43.340  62.480  120.456 1.00 18.44 ? 227  ARG B O     1 
ATOM   4893  C  CB    . ARG J  3 227 ? 41.056  64.591  119.368 1.00 19.91 ? 227  ARG B CB    1 
ATOM   4894  C  CG    . ARG J  3 227 ? 41.241  66.091  119.166 1.00 17.95 ? 227  ARG B CG    1 
ATOM   4895  C  CD    . ARG J  3 227 ? 39.981  66.920  119.364 1.00 21.26 ? 227  ARG B CD    1 
ATOM   4896  N  NE    . ARG J  3 227 ? 40.309  68.348  119.412 1.00 18.37 ? 227  ARG B NE    1 
ATOM   4897  C  CZ    . ARG J  3 227 ? 39.486  69.314  119.012 1.00 21.72 ? 227  ARG B CZ    1 
ATOM   4898  N  NH1   . ARG J  3 227 ? 38.291  68.997  118.529 1.00 21.29 ? 227  ARG B NH1   1 
ATOM   4899  N  NH2   . ARG J  3 227 ? 39.861  70.588  119.097 1.00 22.35 ? 227  ARG B NH2   1 
ATOM   4900  N  N     . ILE J  3 228 ? 41.897  61.456  119.080 1.00 18.50 ? 228  ILE B N     1 
ATOM   4901  C  CA    . ILE J  3 228 ? 42.133  60.138  119.680 1.00 19.19 ? 228  ILE B CA    1 
ATOM   4902  C  C     . ILE J  3 228 ? 43.629  59.778  119.558 1.00 20.15 ? 228  ILE B C     1 
ATOM   4903  O  O     . ILE J  3 228 ? 44.227  59.193  120.470 1.00 16.66 ? 228  ILE B O     1 
ATOM   4904  C  CB    . ILE J  3 228 ? 41.324  59.033  118.942 1.00 18.00 ? 228  ILE B CB    1 
ATOM   4905  C  CG1   . ILE J  3 228 ? 39.819  59.237  119.158 1.00 20.69 ? 228  ILE B CG1   1 
ATOM   4906  C  CG2   . ILE J  3 228 ? 41.773  57.631  119.420 1.00 21.90 ? 228  ILE B CG2   1 
ATOM   4907  C  CD1   . ILE J  3 228 ? 38.952  58.439  118.184 1.00 18.63 ? 228  ILE B CD1   1 
ATOM   4908  N  N     . SER J  3 229 ? 44.237  60.125  118.422 1.00 18.52 ? 229  SER B N     1 
ATOM   4909  C  CA    . SER J  3 229 ? 45.630  59.788  118.175 1.00 17.90 ? 229  SER B CA    1 
ATOM   4910  C  C     . SER J  3 229 ? 46.603  60.466  119.127 1.00 17.82 ? 229  SER B C     1 
ATOM   4911  O  O     . SER J  3 229 ? 47.720  59.974  119.288 1.00 20.38 ? 229  SER B O     1 
ATOM   4912  C  CB    . SER J  3 229 ? 46.019  60.130  116.715 1.00 20.08 ? 229  SER B CB    1 
ATOM   4913  O  OG    . SER J  3 229 ? 46.258  61.514  116.562 1.00 21.60 ? 229  SER B OG    1 
ATOM   4914  N  N     . SER J  3 230 ? 46.189  61.567  119.767 1.00 18.83 ? 230  SER B N     1 
ATOM   4915  C  CA    . SER J  3 230 ? 47.060  62.280  120.703 1.00 21.22 ? 230  SER B CA    1 
ATOM   4916  C  C     . SER J  3 230 ? 47.357  61.426  121.938 1.00 21.16 ? 230  SER B C     1 
ATOM   4917  O  O     . SER J  3 230 ? 48.323  61.716  122.658 1.00 18.78 ? 230  SER B O     1 
ATOM   4918  C  CB    . SER J  3 230 ? 46.472  63.642  121.138 1.00 17.92 ? 230  SER B CB    1 
ATOM   4919  O  OG    . SER J  3 230 ? 45.332  63.516  121.958 1.00 21.00 ? 230  SER B OG    1 
ATOM   4920  N  N     . ILE J  3 231 ? 46.520  60.416  122.194 1.00 19.42 ? 231  ILE B N     1 
ATOM   4921  C  CA    . ILE J  3 231 ? 46.783  59.502  123.303 1.00 19.54 ? 231  ILE B CA    1 
ATOM   4922  C  C     . ILE J  3 231 ? 47.002  58.051  122.837 1.00 20.47 ? 231  ILE B C     1 
ATOM   4923  O  O     . ILE J  3 231 ? 47.709  57.293  123.497 1.00 19.11 ? 231  ILE B O     1 
ATOM   4924  C  CB    . ILE J  3 231 ? 45.676  59.585  124.404 1.00 18.86 ? 231  ILE B CB    1 
ATOM   4925  C  CG1   . ILE J  3 231 ? 46.059  58.702  125.620 1.00 20.51 ? 231  ILE B CG1   1 
ATOM   4926  C  CG2   . ILE J  3 231 ? 44.335  59.161  123.847 1.00 18.27 ? 231  ILE B CG2   1 
ATOM   4927  C  CD1   . ILE J  3 231 ? 47.428  59.088  126.245 1.00 23.27 ? 231  ILE B CD1   1 
ATOM   4928  N  N     . ALA J  3 232 ? 46.433  57.659  121.693 1.00 16.85 ? 232  ALA B N     1 
ATOM   4929  C  CA    . ALA J  3 232 ? 46.585  56.285  121.217 1.00 20.16 ? 232  ALA B CA    1 
ATOM   4930  C  C     . ALA J  3 232 ? 47.917  55.964  120.550 1.00 18.87 ? 232  ALA B C     1 
ATOM   4931  O  O     . ALA J  3 232 ? 48.426  54.860  120.685 1.00 17.17 ? 232  ALA B O     1 
ATOM   4932  C  CB    . ALA J  3 232 ? 45.442  55.915  120.249 1.00 17.56 ? 232  ALA B CB    1 
ATOM   4933  N  N     . LEU J  3 233 ? 48.478  56.904  119.799 1.00 20.52 ? 233  LEU B N     1 
ATOM   4934  C  CA    . LEU J  3 233 ? 49.746  56.621  119.135 1.00 22.08 ? 233  LEU B CA    1 
ATOM   4935  C  C     . LEU J  3 233 ? 50.884  56.581  120.139 1.00 22.33 ? 233  LEU B C     1 
ATOM   4936  O  O     . LEU J  3 233 ? 50.848  57.256  121.169 1.00 25.17 ? 233  LEU B O     1 
ATOM   4937  C  CB    . LEU J  3 233 ? 50.036  57.682  118.065 1.00 23.22 ? 233  LEU B CB    1 
ATOM   4938  C  CG    . LEU J  3 233 ? 49.061  57.703  116.892 1.00 24.25 ? 233  LEU B CG    1 
ATOM   4939  C  CD1   . LEU J  3 233 ? 49.453  58.886  116.000 1.00 21.95 ? 233  LEU B CD1   1 
ATOM   4940  C  CD2   . LEU J  3 233 ? 49.085  56.407  116.108 1.00 26.22 ? 233  LEU B CD2   1 
ATOM   4941  N  N     . GLY J  3 234 ? 51.884  55.773  119.816 1.00 23.91 ? 234  GLY B N     1 
ATOM   4942  C  CA    . GLY J  3 234 ? 53.043  55.644  120.676 1.00 23.24 ? 234  GLY B CA    1 
ATOM   4943  C  C     . GLY J  3 234 ? 52.814  54.453  121.589 1.00 20.42 ? 234  GLY B C     1 
ATOM   4944  O  O     . GLY J  3 234 ? 51.676  53.992  121.757 1.00 21.31 ? 234  GLY B O     1 
ATOM   4945  N  N     . THR J  3 235 ? 53.900  53.933  122.145 1.00 19.52 ? 235  THR B N     1 
ATOM   4946  C  CA    . THR J  3 235 ? 53.802  52.805  123.066 1.00 18.76 ? 235  THR B CA    1 
ATOM   4947  C  C     . THR J  3 235 ? 54.649  53.121  124.281 1.00 20.89 ? 235  THR B C     1 
ATOM   4948  O  O     . THR J  3 235 ? 55.500  54.026  124.258 1.00 20.84 ? 235  THR B O     1 
ATOM   4949  C  CB    . THR J  3 235 ? 54.333  51.490  122.441 1.00 20.08 ? 235  THR B CB    1 
ATOM   4950  O  OG1   . THR J  3 235 ? 55.676  51.681  121.968 1.00 21.35 ? 235  THR B OG1   1 
ATOM   4951  C  CG2   . THR J  3 235 ? 53.431  51.045  121.307 1.00 21.40 ? 235  THR B CG2   1 
ATOM   4952  N  N     . GLY J  3 236 ? 54.409  52.381  125.356 1.00 18.47 ? 236  GLY B N     1 
ATOM   4953  C  CA    . GLY J  3 236 ? 55.213  52.567  126.549 1.00 18.05 ? 236  GLY B CA    1 
ATOM   4954  C  C     . GLY J  3 236 ? 54.449  52.977  127.785 1.00 19.21 ? 236  GLY B C     1 
ATOM   4955  O  O     . GLY J  3 236 ? 54.813  52.598  128.911 1.00 17.24 ? 236  GLY B O     1 
ATOM   4956  N  N     . GLU J  3 237 ? 53.389  53.757  127.598 1.00 17.55 ? 237  GLU B N     1 
ATOM   4957  C  CA    . GLU J  3 237 ? 52.609  54.208  128.753 1.00 18.73 ? 237  GLU B CA    1 
ATOM   4958  C  C     . GLU J  3 237 ? 51.240  53.557  128.794 1.00 16.85 ? 237  GLU B C     1 
ATOM   4959  O  O     . GLU J  3 237 ? 50.805  53.051  129.838 1.00 19.51 ? 237  GLU B O     1 
ATOM   4960  C  CB    . GLU J  3 237 ? 52.370  55.729  128.706 1.00 19.25 ? 237  GLU B CB    1 
ATOM   4961  C  CG    . GLU J  3 237 ? 53.602  56.618  128.638 1.00 28.42 ? 237  GLU B CG    1 
ATOM   4962  C  CD    . GLU J  3 237 ? 54.080  56.953  127.213 1.00 32.30 ? 237  GLU B CD    1 
ATOM   4963  O  OE1   . GLU J  3 237 ? 53.281  56.971  126.239 1.00 27.02 ? 237  GLU B OE1   1 
ATOM   4964  O  OE2   . GLU J  3 237 ? 55.283  57.236  127.077 1.00 33.15 ? 237  GLU B OE2   1 
ATOM   4965  N  N     . ILE J  3 238 ? 50.566  53.591  127.644 1.00 14.39 ? 238  ILE B N     1 
ATOM   4966  C  CA    . ILE J  3 238 ? 49.208  53.095  127.486 1.00 15.37 ? 238  ILE B CA    1 
ATOM   4967  C  C     . ILE J  3 238 ? 49.172  51.760  126.741 1.00 14.19 ? 238  ILE B C     1 
ATOM   4968  O  O     . ILE J  3 238 ? 49.706  51.654  125.635 1.00 17.52 ? 238  ILE B O     1 
ATOM   4969  C  CB    . ILE J  3 238 ? 48.364  54.126  126.661 1.00 17.19 ? 238  ILE B CB    1 
ATOM   4970  C  CG1   . ILE J  3 238 ? 48.434  55.526  127.284 1.00 18.12 ? 238  ILE B CG1   1 
ATOM   4971  C  CG2   . ILE J  3 238 ? 46.943  53.629  126.530 1.00 21.06 ? 238  ILE B CG2   1 
ATOM   4972  C  CD1   . ILE J  3 238 ? 48.052  55.586  128.747 1.00 22.93 ? 238  ILE B CD1   1 
ATOM   4973  N  N     . ASP J  3 239 ? 48.533  50.748  127.334 1.00 13.57 ? 239  ASP B N     1 
ATOM   4974  C  CA    . ASP J  3 239 ? 48.453  49.444  126.674 1.00 14.99 ? 239  ASP B CA    1 
ATOM   4975  C  C     . ASP J  3 239 ? 47.656  49.542  125.367 1.00 17.86 ? 239  ASP B C     1 
ATOM   4976  O  O     . ASP J  3 239 ? 48.063  48.997  124.320 1.00 15.12 ? 239  ASP B O     1 
ATOM   4977  C  CB    . ASP J  3 239 ? 47.744  48.414  127.554 1.00 14.90 ? 239  ASP B CB    1 
ATOM   4978  C  CG    . ASP J  3 239 ? 48.491  48.114  128.837 1.00 16.94 ? 239  ASP B CG    1 
ATOM   4979  O  OD1   . ASP J  3 239 ? 49.611  48.617  129.013 1.00 16.41 ? 239  ASP B OD1   1 
ATOM   4980  O  OD2   . ASP J  3 239 ? 47.929  47.361  129.653 1.00 16.77 ? 239  ASP B OD2   1 
ATOM   4981  N  N     . CYS J  3 240 ? 46.514  50.223  125.436 1.00 16.50 ? 240  CYS B N     1 
ATOM   4982  C  CA    . CYS J  3 240 ? 45.628  50.342  124.273 1.00 17.13 ? 240  CYS B CA    1 
ATOM   4983  C  C     . CYS J  3 240 ? 44.511  51.313  124.630 1.00 18.61 ? 240  CYS B C     1 
ATOM   4984  O  O     . CYS J  3 240 ? 44.203  51.505  125.805 1.00 16.09 ? 240  CYS B O     1 
ATOM   4985  C  CB    . CYS J  3 240 ? 45.019  48.974  123.966 1.00 16.33 ? 240  CYS B CB    1 
ATOM   4986  S  SG    . CYS J  3 240 ? 44.149  48.854  122.332 1.00 19.07 ? 240  CYS B SG    1 
ATOM   4987  N  N     . VAL J  3 241 ? 43.889  51.901  123.608 1.00 15.51 ? 241  VAL B N     1 
ATOM   4988  C  CA    . VAL J  3 241 ? 42.753  52.811  123.779 1.00 16.76 ? 241  VAL B CA    1 
ATOM   4989  C  C     . VAL J  3 241 ? 41.497  52.110  123.230 1.00 18.46 ? 241  VAL B C     1 
ATOM   4990  O  O     . VAL J  3 241 ? 41.560  51.370  122.235 1.00 18.57 ? 241  VAL B O     1 
ATOM   4991  C  CB    . VAL J  3 241 ? 42.996  54.147  123.014 1.00 17.16 ? 241  VAL B CB    1 
ATOM   4992  C  CG1   . VAL J  3 241 ? 41.785  55.069  123.114 1.00 17.68 ? 241  VAL B CG1   1 
ATOM   4993  C  CG2   . VAL J  3 241 ? 44.234  54.825  123.595 1.00 17.53 ? 241  VAL B CG2   1 
ATOM   4994  N  N     . TYR J  3 242 ? 40.368  52.349  123.882 1.00 17.52 ? 242  TYR B N     1 
ATOM   4995  C  CA    . TYR J  3 242 ? 39.097  51.739  123.506 1.00 17.00 ? 242  TYR B CA    1 
ATOM   4996  C  C     . TYR J  3 242 ? 38.089  52.850  123.244 1.00 19.59 ? 242  TYR B C     1 
ATOM   4997  O  O     . TYR J  3 242 ? 37.874  53.716  124.086 1.00 17.44 ? 242  TYR B O     1 
ATOM   4998  C  CB    . TYR J  3 242 ? 38.586  50.835  124.627 1.00 18.57 ? 242  TYR B CB    1 
ATOM   4999  C  CG    . TYR J  3 242 ? 39.518  49.676  124.916 1.00 21.56 ? 242  TYR B CG    1 
ATOM   5000  C  CD1   . TYR J  3 242 ? 40.687  49.867  125.672 1.00 17.76 ? 242  TYR B CD1   1 
ATOM   5001  C  CD2   . TYR J  3 242 ? 39.301  48.415  124.349 1.00 19.68 ? 242  TYR B CD2   1 
ATOM   5002  C  CE1   . TYR J  3 242 ? 41.620  48.845  125.837 1.00 18.78 ? 242  TYR B CE1   1 
ATOM   5003  C  CE2   . TYR J  3 242 ? 40.238  47.374  124.525 1.00 18.84 ? 242  TYR B CE2   1 
ATOM   5004  C  CZ    . TYR J  3 242 ? 41.392  47.599  125.260 1.00 18.69 ? 242  TYR B CZ    1 
ATOM   5005  O  OH    . TYR J  3 242 ? 42.322  46.582  125.415 1.00 18.90 ? 242  TYR B OH    1 
ATOM   5006  N  N     . HIS J  3 243 ? 37.480  52.811  122.061 1.00 19.01 ? 243  HIS B N     1 
ATOM   5007  C  CA    . HIS J  3 243 ? 36.515  53.835  121.685 1.00 19.58 ? 243  HIS B CA    1 
ATOM   5008  C  C     . HIS J  3 243 ? 35.075  53.417  122.031 1.00 20.01 ? 243  HIS B C     1 
ATOM   5009  O  O     . HIS J  3 243 ? 34.707  52.247  121.896 1.00 19.02 ? 243  HIS B O     1 
ATOM   5010  C  CB    . HIS J  3 243 ? 36.661  54.137  120.192 1.00 20.98 ? 243  HIS B CB    1 
ATOM   5011  C  CG    . HIS J  3 243 ? 35.925  55.361  119.761 1.00 20.21 ? 243  HIS B CG    1 
ATOM   5012  N  ND1   . HIS J  3 243 ? 34.630  55.323  119.289 1.00 23.96 ? 243  HIS B ND1   1 
ATOM   5013  C  CD2   . HIS J  3 243 ? 36.280  56.669  119.785 1.00 23.18 ? 243  HIS B CD2   1 
ATOM   5014  C  CE1   . HIS J  3 243 ? 34.221  56.554  119.037 1.00 22.29 ? 243  HIS B CE1   1 
ATOM   5015  N  NE2   . HIS J  3 243 ? 35.200  57.390  119.330 1.00 20.57 ? 243  HIS B NE2   1 
ATOM   5016  N  N     . PHE J  3 244 ? 34.267  54.365  122.505 1.00 19.38 ? 244  PHE B N     1 
ATOM   5017  C  CA    . PHE J  3 244 ? 32.903  54.045  122.919 1.00 21.39 ? 244  PHE B CA    1 
ATOM   5018  C  C     . PHE J  3 244 ? 31.952  53.538  121.825 1.00 21.50 ? 244  PHE B C     1 
ATOM   5019  O  O     . PHE J  3 244 ? 30.942  52.905  122.128 1.00 24.16 ? 244  PHE B O     1 
ATOM   5020  C  CB    . PHE J  3 244 ? 32.279  55.245  123.656 1.00 20.61 ? 244  PHE B CB    1 
ATOM   5021  C  CG    . PHE J  3 244 ? 31.445  56.165  122.777 1.00 23.44 ? 244  PHE B CG    1 
ATOM   5022  C  CD1   . PHE J  3 244 ? 30.105  56.387  123.087 1.00 24.64 ? 244  PHE B CD1   1 
ATOM   5023  C  CD2   . PHE J  3 244 ? 32.008  56.836  121.698 1.00 23.13 ? 244  PHE B CD2   1 
ATOM   5024  C  CE1   . PHE J  3 244 ? 29.334  57.279  122.326 1.00 24.65 ? 244  PHE B CE1   1 
ATOM   5025  C  CE2   . PHE J  3 244 ? 31.244  57.732  120.931 1.00 26.96 ? 244  PHE B CE2   1 
ATOM   5026  C  CZ    . PHE J  3 244 ? 29.915  57.949  121.249 1.00 26.25 ? 244  PHE B CZ    1 
ATOM   5027  N  N     . ALA J  3 245 ? 32.307  53.792  120.572 1.00 23.11 ? 245  ALA B N     1 
ATOM   5028  C  CA    . ALA J  3 245 ? 31.462  53.385  119.445 1.00 24.96 ? 245  ALA B CA    1 
ATOM   5029  C  C     . ALA J  3 245 ? 32.320  53.276  118.199 1.00 23.53 ? 245  ALA B C     1 
ATOM   5030  O  O     . ALA J  3 245 ? 32.155  54.016  117.226 1.00 25.71 ? 245  ALA B O     1 
ATOM   5031  C  CB    . ALA J  3 245 ? 30.331  54.434  119.245 1.00 25.00 ? 245  ALA B CB    1 
ATOM   5032  N  N     . LEU J  3 246 ? 33.243  52.332  118.217 1.00 22.99 ? 246  LEU B N     1 
ATOM   5033  C  CA    . LEU J  3 246 ? 34.178  52.167  117.116 1.00 22.93 ? 246  LEU B CA    1 
ATOM   5034  C  C     . LEU J  3 246 ? 33.584  51.822  115.762 1.00 24.84 ? 246  LEU B C     1 
ATOM   5035  O  O     . LEU J  3 246 ? 33.995  52.391  114.748 1.00 25.81 ? 246  LEU B O     1 
ATOM   5036  C  CB    . LEU J  3 246 ? 35.228  51.112  117.473 1.00 21.91 ? 246  LEU B CB    1 
ATOM   5037  C  CG    . LEU J  3 246 ? 36.437  51.103  116.549 1.00 24.54 ? 246  LEU B CG    1 
ATOM   5038  C  CD1   . LEU J  3 246 ? 37.401  52.184  117.005 1.00 26.77 ? 246  LEU B CD1   1 
ATOM   5039  C  CD2   . LEU J  3 246 ? 37.121  49.735  116.582 1.00 25.25 ? 246  LEU B CD2   1 
ATOM   5040  N  N     . TYR J  3 247 ? 32.646  50.878  115.752 1.00 24.63 ? 247  TYR B N     1 
ATOM   5041  C  CA    . TYR J  3 247 ? 32.019  50.434  114.504 1.00 27.68 ? 247  TYR B CA    1 
ATOM   5042  C  C     . TYR J  3 247 ? 31.305  51.599  113.835 1.00 27.29 ? 247  TYR B C     1 
ATOM   5043  O  O     . TYR J  3 247 ? 31.366  51.752  112.619 1.00 29.71 ? 247  TYR B O     1 
ATOM   5044  C  CB    . TYR J  3 247 ? 31.010  49.328  114.792 1.00 27.79 ? 247  TYR B CB    1 
ATOM   5045  C  CG    . TYR J  3 247 ? 31.544  48.231  115.691 1.00 28.82 ? 247  TYR B CG    1 
ATOM   5046  C  CD1   . TYR J  3 247 ? 30.717  47.623  116.628 1.00 25.15 ? 247  TYR B CD1   1 
ATOM   5047  C  CD2   . TYR J  3 247 ? 32.877  47.810  115.609 1.00 30.63 ? 247  TYR B CD2   1 
ATOM   5048  C  CE1   . TYR J  3 247 ? 31.198  46.614  117.473 1.00 28.07 ? 247  TYR B CE1   1 
ATOM   5049  C  CE2   . TYR J  3 247 ? 33.366  46.798  116.456 1.00 28.05 ? 247  TYR B CE2   1 
ATOM   5050  C  CZ    . TYR J  3 247 ? 32.523  46.214  117.379 1.00 28.97 ? 247  TYR B CZ    1 
ATOM   5051  O  OH    . TYR J  3 247 ? 32.993  45.247  118.246 1.00 26.68 ? 247  TYR B OH    1 
ATOM   5052  N  N     . GLU J  3 248 ? 30.629  52.399  114.657 1.00 28.68 ? 248  GLU B N     1 
ATOM   5053  C  CA    . GLU J  3 248 ? 29.881  53.560  114.189 1.00 25.26 ? 248  GLU B CA    1 
ATOM   5054  C  C     . GLU J  3 248 ? 30.834  54.641  113.697 1.00 27.06 ? 248  GLU B C     1 
ATOM   5055  O  O     . GLU J  3 248 ? 30.566  55.316  112.705 1.00 28.84 ? 248  GLU B O     1 
ATOM   5056  C  CB    . GLU J  3 248 ? 29.003  54.095  115.317 1.00 26.92 ? 248  GLU B CB    1 
ATOM   5057  C  CG    . GLU J  3 248 ? 27.882  53.159  115.778 1.00 22.27 ? 248  GLU B CG    1 
ATOM   5058  C  CD    . GLU J  3 248 ? 28.346  52.071  116.766 1.00 27.98 ? 248  GLU B CD    1 
ATOM   5059  O  OE1   . GLU J  3 248 ? 29.490  52.137  117.272 1.00 27.53 ? 248  GLU B OE1   1 
ATOM   5060  O  OE2   . GLU J  3 248 ? 27.548  51.155  117.051 1.00 27.48 ? 248  GLU B OE2   1 
ATOM   5061  N  N     . LEU J  3 249 ? 31.950  54.834  114.399 1.00 25.22 ? 249  LEU B N     1 
ATOM   5062  C  CA    . LEU J  3 249 ? 32.938  55.807  113.953 1.00 24.21 ? 249  LEU B CA    1 
ATOM   5063  C  C     . LEU J  3 249 ? 33.442  55.432  112.565 1.00 25.10 ? 249  LEU B C     1 
ATOM   5064  O  O     . LEU J  3 249 ? 33.545  56.282  111.674 1.00 26.63 ? 249  LEU B O     1 
ATOM   5065  C  CB    . LEU J  3 249 ? 34.144  55.844  114.913 1.00 24.71 ? 249  LEU B CB    1 
ATOM   5066  C  CG    . LEU J  3 249 ? 35.344  56.664  114.446 1.00 25.30 ? 249  LEU B CG    1 
ATOM   5067  C  CD1   . LEU J  3 249 ? 34.942  58.111  114.189 1.00 25.81 ? 249  LEU B CD1   1 
ATOM   5068  C  CD2   . LEU J  3 249 ? 36.442  56.577  115.522 1.00 27.14 ? 249  LEU B CD2   1 
ATOM   5069  N  N     . GLU J  3 250 ? 33.767  54.154  112.369 1.00 27.26 ? 250  GLU B N     1 
ATOM   5070  C  CA    . GLU J  3 250 ? 34.292  53.728  111.081 1.00 29.54 ? 250  GLU B CA    1 
ATOM   5071  C  C     . GLU J  3 250 ? 33.268  53.927  109.955 1.00 27.63 ? 250  GLU B C     1 
ATOM   5072  O  O     . GLU J  3 250 ? 33.616  54.410  108.887 1.00 31.13 ? 250  GLU B O     1 
ATOM   5073  C  CB    . GLU J  3 250 ? 34.709  52.262  111.123 1.00 31.33 ? 250  GLU B CB    1 
ATOM   5074  C  CG    . GLU J  3 250 ? 35.606  51.898  109.979 1.00 39.02 ? 250  GLU B CG    1 
ATOM   5075  C  CD    . GLU J  3 250 ? 35.231  50.578  109.362 1.00 50.99 ? 250  GLU B CD    1 
ATOM   5076  O  OE1   . GLU J  3 250 ? 35.309  49.542  110.066 1.00 53.59 ? 250  GLU B OE1   1 
ATOM   5077  O  OE2   . GLU J  3 250 ? 34.852  50.583  108.168 1.00 52.09 ? 250  GLU B OE2   1 
ATOM   5078  N  N     . GLN J  3 251 ? 32.025  53.561  110.223 1.00 31.39 ? 251  GLN B N     1 
ATOM   5079  C  CA    . GLN J  3 251 ? 30.938  53.684  109.254 1.00 34.41 ? 251  GLN B CA    1 
ATOM   5080  C  C     . GLN J  3 251 ? 30.736  55.131  108.803 1.00 36.70 ? 251  GLN B C     1 
ATOM   5081  O  O     . GLN J  3 251 ? 30.671  55.404  107.597 1.00 36.20 ? 251  GLN B O     1 
ATOM   5082  C  CB    . GLN J  3 251 ? 29.644  53.143  109.859 1.00 38.90 ? 251  GLN B CB    1 
ATOM   5083  C  CG    . GLN J  3 251 ? 28.503  52.967  108.870 1.00 48.40 ? 251  GLN B CG    1 
ATOM   5084  C  CD    . GLN J  3 251 ? 27.297  52.288  109.497 1.00 53.15 ? 251  GLN B CD    1 
ATOM   5085  O  OE1   . GLN J  3 251 ? 27.402  51.187  110.046 1.00 56.40 ? 251  GLN B OE1   1 
ATOM   5086  N  NE2   . GLN J  3 251 ? 26.140  52.939  109.413 1.00 56.76 ? 251  GLN B NE2   1 
ATOM   5087  N  N     . ILE J  3 252 ? 30.641  56.062  109.755 1.00 32.68 ? 252  ILE B N     1 
ATOM   5088  C  CA    . ILE J  3 252 ? 30.435  57.453  109.384 1.00 33.57 ? 252  ILE B CA    1 
ATOM   5089  C  C     . ILE J  3 252 ? 31.647  58.031  108.677 1.00 32.70 ? 252  ILE B C     1 
ATOM   5090  O  O     . ILE J  3 252 ? 31.514  58.867  107.780 1.00 35.86 ? 252  ILE B O     1 
ATOM   5091  C  CB    . ILE J  3 252 ? 30.079  58.343  110.591 1.00 35.14 ? 252  ILE B CB    1 
ATOM   5092  C  CG1   . ILE J  3 252 ? 29.906  59.779  110.100 1.00 39.28 ? 252  ILE B CG1   1 
ATOM   5093  C  CG2   . ILE J  3 252 ? 31.178  58.305  111.642 1.00 37.38 ? 252  ILE B CG2   1 
ATOM   5094  C  CD1   . ILE J  3 252 ? 29.587  60.748  111.167 1.00 44.65 ? 252  ILE B CD1   1 
ATOM   5095  N  N     . LEU J  3 253 ? 32.840  57.595  109.067 1.00 32.97 ? 253  LEU B N     1 
ATOM   5096  C  CA    . LEU J  3 253 ? 34.043  58.083  108.415 1.00 28.96 ? 253  LEU B CA    1 
ATOM   5097  C  C     . LEU J  3 253 ? 34.034  57.662  106.933 1.00 31.76 ? 253  LEU B C     1 
ATOM   5098  O  O     . LEU J  3 253 ? 34.526  58.383  106.063 1.00 31.46 ? 253  LEU B O     1 
ATOM   5099  C  CB    . LEU J  3 253 ? 35.299  57.537  109.115 1.00 31.16 ? 253  LEU B CB    1 
ATOM   5100  C  CG    . LEU J  3 253 ? 35.720  58.174  110.448 1.00 28.39 ? 253  LEU B CG    1 
ATOM   5101  C  CD1   . LEU J  3 253 ? 36.899  57.393  111.039 1.00 25.93 ? 253  LEU B CD1   1 
ATOM   5102  C  CD2   . LEU J  3 253 ? 36.105  59.637  110.229 1.00 30.86 ? 253  LEU B CD2   1 
ATOM   5103  N  N     . GLN J  3 254 ? 33.468  56.497  106.648 1.00 33.76 ? 254  GLN B N     1 
ATOM   5104  C  CA    . GLN J  3 254 ? 33.412  56.030  105.267 1.00 37.35 ? 254  GLN B CA    1 
ATOM   5105  C  C     . GLN J  3 254 ? 32.348  56.794  104.494 1.00 37.30 ? 254  GLN B C     1 
ATOM   5106  O  O     . GLN J  3 254 ? 32.588  57.222  103.369 1.00 40.75 ? 254  GLN B O     1 
ATOM   5107  C  CB    . GLN J  3 254 ? 33.120  54.532  105.223 1.00 38.50 ? 254  GLN B CB    1 
ATOM   5108  C  CG    . GLN J  3 254 ? 34.222  53.704  105.848 1.00 47.58 ? 254  GLN B CG    1 
ATOM   5109  C  CD    . GLN J  3 254 ? 33.890  52.235  105.921 1.00 51.33 ? 254  GLN B CD    1 
ATOM   5110  O  OE1   . GLN J  3 254 ? 32.801  51.847  106.356 1.00 54.83 ? 254  GLN B OE1   1 
ATOM   5111  N  NE2   . GLN J  3 254 ? 34.838  51.399  105.509 1.00 55.31 ? 254  GLN B NE2   1 
ATOM   5112  N  N     . SER J  3 255 ? 31.189  56.980  105.114 1.00 39.33 ? 255  SER B N     1 
ATOM   5113  C  CA    . SER J  3 255 ? 30.075  57.693  104.491 1.00 41.29 ? 255  SER B CA    1 
ATOM   5114  C  C     . SER J  3 255 ? 30.367  59.158  104.181 1.00 42.71 ? 255  SER B C     1 
ATOM   5115  O  O     . SER J  3 255 ? 29.778  59.725  103.261 1.00 42.67 ? 255  SER B O     1 
ATOM   5116  C  CB    . SER J  3 255 ? 28.834  57.618  105.383 1.00 43.67 ? 255  SER B CB    1 
ATOM   5117  O  OG    . SER J  3 255 ? 28.397  56.278  105.546 1.00 51.20 ? 255  SER B OG    1 
ATOM   5118  N  N     . LEU J  3 256 ? 31.255  59.781  104.950 1.00 40.78 ? 256  LEU B N     1 
ATOM   5119  C  CA    . LEU J  3 256 ? 31.589  61.186  104.728 1.00 39.22 ? 256  LEU B CA    1 
ATOM   5120  C  C     . LEU J  3 256 ? 32.826  61.302  103.859 1.00 38.43 ? 256  LEU B C     1 
ATOM   5121  O  O     . LEU J  3 256 ? 33.238  62.398  103.483 1.00 38.37 ? 256  LEU B O     1 
ATOM   5122  C  CB    . LEU J  3 256 ? 31.826  61.899  106.067 1.00 39.40 ? 256  LEU B CB    1 
ATOM   5123  C  CG    . LEU J  3 256 ? 30.675  61.849  107.083 1.00 38.79 ? 256  LEU B CG    1 
ATOM   5124  C  CD1   . LEU J  3 256 ? 31.135  62.451  108.413 1.00 40.14 ? 256  LEU B CD1   1 
ATOM   5125  C  CD2   . LEU J  3 256 ? 29.458  62.604  106.542 1.00 42.98 ? 256  LEU B CD2   1 
ATOM   5126  N  N     . ASN J  3 257 ? 33.417  60.159  103.534 1.00 40.73 ? 257  ASN B N     1 
ATOM   5127  C  CA    . ASN J  3 257 ? 34.623  60.117  102.721 1.00 42.30 ? 257  ASN B CA    1 
ATOM   5128  C  C     . ASN J  3 257 ? 35.742  61.011  103.251 1.00 40.22 ? 257  ASN B C     1 
ATOM   5129  O  O     . ASN J  3 257 ? 36.402  61.723  102.492 1.00 37.85 ? 257  ASN B O     1 
ATOM   5130  C  CB    . ASN J  3 257 ? 34.291  60.480  101.267 1.00 47.94 ? 257  ASN B CB    1 
ATOM   5131  C  CG    . ASN J  3 257 ? 33.343  59.482  100.629 1.00 53.42 ? 257  ASN B CG    1 
ATOM   5132  O  OD1   . ASN J  3 257 ? 33.673  58.298  100.478 1.00 56.27 ? 257  ASN B OD1   1 
ATOM   5133  N  ND2   . ASN J  3 257 ? 32.152  59.948  100.259 1.00 54.88 ? 257  ASN B ND2   1 
ATOM   5134  N  N     . TYR J  3 258 ? 35.953  60.979  104.566 1.00 38.87 ? 258  TYR B N     1 
ATOM   5135  C  CA    . TYR J  3 258 ? 37.025  61.763  105.181 1.00 38.09 ? 258  TYR B CA    1 
ATOM   5136  C  C     . TYR J  3 258 ? 38.231  60.844  105.094 1.00 39.70 ? 258  TYR B C     1 
ATOM   5137  O  O     . TYR J  3 258 ? 38.525  60.096  106.031 1.00 37.20 ? 258  TYR B O     1 
ATOM   5138  C  CB    . TYR J  3 258 ? 36.700  62.072  106.647 1.00 39.83 ? 258  TYR B CB    1 
ATOM   5139  C  CG    . TYR J  3 258 ? 35.682  63.172  106.869 1.00 40.29 ? 258  TYR B CG    1 
ATOM   5140  C  CD1   . TYR J  3 258 ? 35.211  63.453  108.154 1.00 42.00 ? 258  TYR B CD1   1 
ATOM   5141  C  CD2   . TYR J  3 258 ? 35.201  63.944  105.809 1.00 41.52 ? 258  TYR B CD2   1 
ATOM   5142  C  CE1   . TYR J  3 258 ? 34.291  64.471  108.384 1.00 38.86 ? 258  TYR B CE1   1 
ATOM   5143  C  CE2   . TYR J  3 258 ? 34.275  64.968  106.028 1.00 35.88 ? 258  TYR B CE2   1 
ATOM   5144  C  CZ    . TYR J  3 258 ? 33.826  65.226  107.316 1.00 38.56 ? 258  TYR B CZ    1 
ATOM   5145  O  OH    . TYR J  3 258 ? 32.915  66.235  107.555 1.00 35.63 ? 258  TYR B OH    1 
ATOM   5146  N  N     . GLU J  3 259 ? 38.917  60.913  103.959 1.00 37.63 ? 259  GLU B N     1 
ATOM   5147  C  CA    . GLU J  3 259 ? 40.064  60.066  103.658 1.00 41.54 ? 259  GLU B CA    1 
ATOM   5148  C  C     . GLU J  3 259 ? 41.256  60.083  104.613 1.00 38.60 ? 259  GLU B C     1 
ATOM   5149  O  O     . GLU J  3 259 ? 41.754  59.022  104.984 1.00 41.17 ? 259  GLU B O     1 
ATOM   5150  C  CB    . GLU J  3 259 ? 40.549  60.357  102.236 1.00 43.66 ? 259  GLU B CB    1 
ATOM   5151  C  CG    . GLU J  3 259 ? 41.536  59.329  101.704 1.00 53.93 ? 259  GLU B CG    1 
ATOM   5152  C  CD    . GLU J  3 259 ? 41.874  59.529  100.226 1.00 60.04 ? 259  GLU B CD    1 
ATOM   5153  O  OE1   . GLU J  3 259 ? 41.304  60.450  99.588  1.00 60.03 ? 259  GLU B OE1   1 
ATOM   5154  O  OE2   . GLU J  3 259 ? 42.712  58.755  99.705  1.00 60.03 ? 259  GLU B OE2   1 
ATOM   5155  N  N     . ASP J  3 260 ? 41.739  61.266  104.976 1.00 38.53 ? 260  ASP B N     1 
ATOM   5156  C  CA    . ASP J  3 260 ? 42.871  61.366  105.894 1.00 39.26 ? 260  ASP B CA    1 
ATOM   5157  C  C     . ASP J  3 260 ? 42.497  60.765  107.252 1.00 37.20 ? 260  ASP B C     1 
ATOM   5158  O  O     . ASP J  3 260 ? 43.253  59.981  107.821 1.00 35.35 ? 260  ASP B O     1 
ATOM   5159  C  CB    . ASP J  3 260 ? 43.294  62.831  106.087 1.00 40.51 ? 260  ASP B CB    1 
ATOM   5160  C  CG    . ASP J  3 260 ? 43.908  63.439  104.834 1.00 45.54 ? 260  ASP B CG    1 
ATOM   5161  O  OD1   . ASP J  3 260 ? 44.088  62.707  103.836 1.00 43.80 ? 260  ASP B OD1   1 
ATOM   5162  O  OD2   . ASP J  3 260 ? 44.220  64.651  104.850 1.00 48.79 ? 260  ASP B OD2   1 
ATOM   5163  N  N     . ALA J  3 261 ? 41.328  61.139  107.763 1.00 33.55 ? 261  ALA B N     1 
ATOM   5164  C  CA    . ALA J  3 261 ? 40.861  60.636  109.052 1.00 31.82 ? 261  ALA B CA    1 
ATOM   5165  C  C     . ALA J  3 261 ? 40.625  59.126  109.016 1.00 35.26 ? 261  ALA B C     1 
ATOM   5166  O  O     . ALA J  3 261 ? 40.777  58.445  110.034 1.00 33.90 ? 261  ALA B O     1 
ATOM   5167  C  CB    . ALA J  3 261 ? 39.587  61.360  109.460 1.00 28.64 ? 261  ALA B CB    1 
ATOM   5168  N  N     . LEU J  3 262 ? 40.234  58.592  107.860 1.00 31.69 ? 262  LEU B N     1 
ATOM   5169  C  CA    . LEU J  3 262 ? 40.017  57.155  107.745 1.00 33.15 ? 262  LEU B CA    1 
ATOM   5170  C  C     . LEU J  3 262 ? 41.369  56.467  107.797 1.00 32.32 ? 262  LEU B C     1 
ATOM   5171  O  O     . LEU J  3 262 ? 41.527  55.419  108.444 1.00 33.19 ? 262  LEU B O     1 
ATOM   5172  C  CB    . LEU J  3 262 ? 39.337  56.803  106.424 1.00 35.14 ? 262  LEU B CB    1 
ATOM   5173  C  CG    . LEU J  3 262 ? 37.910  56.286  106.523 1.00 37.21 ? 262  LEU B CG    1 
ATOM   5174  C  CD1   . LEU J  3 262 ? 37.399  56.014  105.118 1.00 41.15 ? 262  LEU B CD1   1 
ATOM   5175  C  CD2   . LEU J  3 262 ? 37.852  55.026  107.365 1.00 37.14 ? 262  LEU B CD2   1 
ATOM   5176  N  N     . ASP J  3 263 ? 42.341  57.052  107.103 1.00 31.49 ? 263  ASP B N     1 
ATOM   5177  C  CA    . ASP J  3 263 ? 43.686  56.501  107.083 1.00 33.12 ? 263  ASP B CA    1 
ATOM   5178  C  C     . ASP J  3 263 ? 44.205  56.428  108.527 1.00 34.47 ? 263  ASP B C     1 
ATOM   5179  O  O     . ASP J  3 263 ? 44.734  55.400  108.942 1.00 33.85 ? 263  ASP B O     1 
ATOM   5180  C  CB    . ASP J  3 263 ? 44.641  57.382  106.271 1.00 36.38 ? 263  ASP B CB    1 
ATOM   5181  C  CG    . ASP J  3 263 ? 44.455  57.235  104.764 1.00 42.11 ? 263  ASP B CG    1 
ATOM   5182  O  OD1   . ASP J  3 263 ? 43.648  56.377  104.336 1.00 43.72 ? 263  ASP B OD1   1 
ATOM   5183  O  OD2   . ASP J  3 263 ? 45.131  57.978  104.017 1.00 43.30 ? 263  ASP B OD2   1 
ATOM   5184  N  N     . LEU J  3 264 ? 44.050  57.518  109.275 1.00 30.30 ? 264  LEU B N     1 
ATOM   5185  C  CA    . LEU J  3 264 ? 44.535  57.563  110.656 1.00 29.18 ? 264  LEU B CA    1 
ATOM   5186  C  C     . LEU J  3 264 ? 43.815  56.533  111.528 1.00 30.22 ? 264  LEU B C     1 
ATOM   5187  O  O     . LEU J  3 264 ? 44.446  55.882  112.378 1.00 28.09 ? 264  LEU B O     1 
ATOM   5188  C  CB    . LEU J  3 264 ? 44.396  58.988  111.236 1.00 27.40 ? 264  LEU B CB    1 
ATOM   5189  C  CG    . LEU J  3 264 ? 44.937  59.219  112.669 1.00 27.69 ? 264  LEU B CG    1 
ATOM   5190  C  CD1   . LEU J  3 264 ? 46.420  58.812  112.793 1.00 25.97 ? 264  LEU B CD1   1 
ATOM   5191  C  CD2   . LEU J  3 264 ? 44.785  60.680  113.027 1.00 26.48 ? 264  LEU B CD2   1 
ATOM   5192  N  N     . PHE J  3 265 ? 42.508  56.384  111.318 1.00 24.02 ? 265  PHE B N     1 
ATOM   5193  C  CA    . PHE J  3 265 ? 41.694  55.414  112.047 1.00 25.60 ? 265  PHE B CA    1 
ATOM   5194  C  C     . PHE J  3 265 ? 42.313  54.016  111.879 1.00 32.03 ? 265  PHE B C     1 
ATOM   5195  O  O     . PHE J  3 265 ? 42.610  53.322  112.854 1.00 26.56 ? 265  PHE B O     1 
ATOM   5196  C  CB    . PHE J  3 265 ? 40.260  55.418  111.484 1.00 25.21 ? 265  PHE B CB    1 
ATOM   5197  C  CG    . PHE J  3 265 ? 39.345  54.415  112.116 1.00 24.40 ? 265  PHE B CG    1 
ATOM   5198  C  CD1   . PHE J  3 265 ? 38.674  54.706  113.301 1.00 26.44 ? 265  PHE B CD1   1 
ATOM   5199  C  CD2   . PHE J  3 265 ? 39.117  53.176  111.513 1.00 24.91 ? 265  PHE B CD2   1 
ATOM   5200  C  CE1   . PHE J  3 265 ? 37.793  53.791  113.863 1.00 25.25 ? 265  PHE B CE1   1 
ATOM   5201  C  CE2   . PHE J  3 265 ? 38.243  52.262  112.069 1.00 25.24 ? 265  PHE B CE2   1 
ATOM   5202  C  CZ    . PHE J  3 265 ? 37.573  52.568  113.249 1.00 24.34 ? 265  PHE B CZ    1 
ATOM   5203  N  N     . TYR J  3 266 ? 42.505  53.602  110.630 1.00 28.95 ? 266  TYR B N     1 
ATOM   5204  C  CA    . TYR J  3 266 ? 43.078  52.292  110.352 1.00 29.87 ? 266  TYR B CA    1 
ATOM   5205  C  C     . TYR J  3 266 ? 44.496  52.109  110.844 1.00 27.68 ? 266  TYR B C     1 
ATOM   5206  O  O     . TYR J  3 266 ? 44.886  51.008  111.220 1.00 28.24 ? 266  TYR B O     1 
ATOM   5207  C  CB    . TYR J  3 266 ? 42.974  51.982  108.854 1.00 30.64 ? 266  TYR B CB    1 
ATOM   5208  C  CG    . TYR J  3 266 ? 41.589  51.510  108.529 1.00 33.82 ? 266  TYR B CG    1 
ATOM   5209  C  CD1   . TYR J  3 266 ? 40.749  52.246  107.695 1.00 36.74 ? 266  TYR B CD1   1 
ATOM   5210  C  CD2   . TYR J  3 266 ? 41.064  50.392  109.171 1.00 34.22 ? 266  TYR B CD2   1 
ATOM   5211  C  CE1   . TYR J  3 266 ? 39.412  51.879  107.524 1.00 41.99 ? 266  TYR B CE1   1 
ATOM   5212  C  CE2   . TYR J  3 266 ? 39.743  50.020  109.011 1.00 41.01 ? 266  TYR B CE2   1 
ATOM   5213  C  CZ    . TYR J  3 266 ? 38.917  50.766  108.192 1.00 39.30 ? 266  TYR B CZ    1 
ATOM   5214  O  OH    . TYR J  3 266 ? 37.589  50.409  108.084 1.00 44.97 ? 266  TYR B OH    1 
ATOM   5215  N  N     . ILE J  3 267 ? 45.278  53.176  110.840 1.00 25.96 ? 267  ILE B N     1 
ATOM   5216  C  CA    . ILE J  3 267 ? 46.637  53.074  111.334 1.00 26.81 ? 267  ILE B CA    1 
ATOM   5217  C  C     . ILE J  3 267 ? 46.536  52.698  112.818 1.00 26.88 ? 267  ILE B C     1 
ATOM   5218  O  O     . ILE J  3 267 ? 47.225  51.799  113.288 1.00 27.70 ? 267  ILE B O     1 
ATOM   5219  C  CB    . ILE J  3 267 ? 47.377  54.399  111.176 1.00 30.17 ? 267  ILE B CB    1 
ATOM   5220  C  CG1   . ILE J  3 267 ? 47.792  54.571  109.709 1.00 27.39 ? 267  ILE B CG1   1 
ATOM   5221  C  CG2   . ILE J  3 267 ? 48.598  54.451  112.111 1.00 31.30 ? 267  ILE B CG2   1 
ATOM   5222  C  CD1   . ILE J  3 267 ? 48.427  55.894  109.425 1.00 32.46 ? 267  ILE B CD1   1 
ATOM   5223  N  N     . MET J  3 268 ? 45.657  53.373  113.547 1.00 25.27 ? 268  MET B N     1 
ATOM   5224  C  CA    . MET J  3 268 ? 45.515  53.067  114.972 1.00 22.85 ? 268  MET B CA    1 
ATOM   5225  C  C     . MET J  3 268 ? 44.890  51.699  115.215 1.00 26.91 ? 268  MET B C     1 
ATOM   5226  O  O     . MET J  3 268 ? 45.304  50.977  116.123 1.00 25.62 ? 268  MET B O     1 
ATOM   5227  C  CB    . MET J  3 268 ? 44.675  54.148  115.674 1.00 22.72 ? 268  MET B CB    1 
ATOM   5228  C  CG    . MET J  3 268 ? 45.326  55.519  115.701 1.00 21.80 ? 268  MET B CG    1 
ATOM   5229  S  SD    . MET J  3 268 ? 44.397  56.705  116.657 1.00 22.02 ? 268  MET B SD    1 
ATOM   5230  C  CE    . MET J  3 268 ? 43.014  57.123  115.496 1.00 20.76 ? 268  MET B CE    1 
ATOM   5231  N  N     . VAL J  3 269 ? 43.916  51.321  114.391 1.00 24.81 ? 269  VAL B N     1 
ATOM   5232  C  CA    . VAL J  3 269 ? 43.230  50.047  114.566 1.00 25.60 ? 269  VAL B CA    1 
ATOM   5233  C  C     . VAL J  3 269 ? 44.071  48.865  114.085 1.00 29.66 ? 269  VAL B C     1 
ATOM   5234  O  O     . VAL J  3 269 ? 44.198  47.876  114.804 1.00 28.89 ? 269  VAL B O     1 
ATOM   5235  C  CB    . VAL J  3 269 ? 41.845  50.059  113.863 1.00 25.08 ? 269  VAL B CB    1 
ATOM   5236  C  CG1   . VAL J  3 269 ? 41.231  48.682  113.882 1.00 27.14 ? 269  VAL B CG1   1 
ATOM   5237  C  CG2   . VAL J  3 269 ? 40.913  51.038  114.579 1.00 23.21 ? 269  VAL B CG2   1 
ATOM   5238  N  N     . ASN J  3 270 ? 44.644  48.960  112.885 1.00 29.07 ? 270  ASN B N     1 
ATOM   5239  C  CA    . ASN J  3 270 ? 45.482  47.872  112.389 1.00 31.88 ? 270  ASN B CA    1 
ATOM   5240  C  C     . ASN J  3 270 ? 46.769  47.826  113.202 1.00 30.95 ? 270  ASN B C     1 
ATOM   5241  O  O     . ASN J  3 270 ? 47.410  46.778  113.307 1.00 32.86 ? 270  ASN B O     1 
ATOM   5242  C  CB    . ASN J  3 270 ? 45.824  48.068  110.912 1.00 35.26 ? 270  ASN B CB    1 
ATOM   5243  C  CG    . ASN J  3 270 ? 44.607  48.011  110.034 1.00 32.80 ? 270  ASN B CG    1 
ATOM   5244  O  OD1   . ASN J  3 270 ? 43.656  47.294  110.338 1.00 38.64 ? 270  ASN B OD1   1 
ATOM   5245  N  ND2   . ASN J  3 270 ? 44.630  48.748  108.927 1.00 36.20 ? 270  ASN B ND2   1 
ATOM   5246  N  N     . GLY J  3 271 ? 47.137  48.972  113.774 1.00 26.94 ? 271  GLY B N     1 
ATOM   5247  C  CA    . GLY J  3 271 ? 48.347  49.076  114.575 1.00 26.12 ? 271  GLY B CA    1 
ATOM   5248  C  C     . GLY J  3 271 ? 48.145  48.725  116.045 1.00 22.83 ? 271  GLY B C     1 
ATOM   5249  O  O     . GLY J  3 271 ? 49.011  49.034  116.863 1.00 26.59 ? 271  GLY B O     1 
ATOM   5250  N  N     . LYS J  3 272 ? 47.006  48.123  116.376 1.00 24.93 ? 272  LYS B N     1 
ATOM   5251  C  CA    . LYS J  3 272 ? 46.712  47.699  117.759 1.00 26.00 ? 272  LYS B CA    1 
ATOM   5252  C  C     . LYS J  3 272 ? 46.836  48.779  118.837 1.00 24.28 ? 272  LYS B C     1 
ATOM   5253  O  O     . LYS J  3 272 ? 47.319  48.525  119.974 1.00 22.12 ? 272  LYS B O     1 
ATOM   5254  C  CB    . LYS J  3 272 ? 47.577  46.484  118.113 1.00 28.86 ? 272  LYS B CB    1 
ATOM   5255  C  CG    . LYS J  3 272 ? 47.465  45.409  117.041 1.00 30.80 ? 272  LYS B CG    1 
ATOM   5256  C  CD    . LYS J  3 272 ? 47.803  44.033  117.547 1.00 38.11 ? 272  LYS B CD    1 
ATOM   5257  C  CE    . LYS J  3 272 ? 49.281  43.869  117.818 1.00 43.91 ? 272  LYS B CE    1 
ATOM   5258  N  NZ    . LYS J  3 272 ? 49.566  42.423  117.984 1.00 44.20 ? 272  LYS B NZ    1 
ATOM   5259  N  N     . ARG J  3 273 ? 46.389  49.982  118.488 1.00 20.85 ? 273  ARG B N     1 
ATOM   5260  C  CA    . ARG J  3 273 ? 46.388  51.116  119.417 1.00 20.20 ? 273  ARG B CA    1 
ATOM   5261  C  C     . ARG J  3 273 ? 44.962  51.525  119.793 1.00 21.01 ? 273  ARG B C     1 
ATOM   5262  O  O     . ARG J  3 273 ? 44.741  52.256  120.771 1.00 21.14 ? 273  ARG B O     1 
ATOM   5263  C  CB    . ARG J  3 273 ? 47.098  52.337  118.800 1.00 20.13 ? 273  ARG B CB    1 
ATOM   5264  C  CG    . ARG J  3 273 ? 48.519  52.093  118.296 1.00 22.27 ? 273  ARG B CG    1 
ATOM   5265  C  CD    . ARG J  3 273 ? 49.310  51.210  119.266 1.00 20.28 ? 273  ARG B CD    1 
ATOM   5266  N  NE    . ARG J  3 273 ? 49.655  51.886  120.518 1.00 18.78 ? 273  ARG B NE    1 
ATOM   5267  C  CZ    . ARG J  3 273 ? 49.479  51.325  121.718 1.00 18.91 ? 273  ARG B CZ    1 
ATOM   5268  N  NH1   . ARG J  3 273 ? 48.952  50.103  121.808 1.00 17.66 ? 273  ARG B NH1   1 
ATOM   5269  N  NH2   . ARG J  3 273 ? 49.845  51.980  122.815 1.00 18.82 ? 273  ARG B NH2   1 
ATOM   5270  N  N     . LEU J  3 274 ? 43.993  51.060  119.016 1.00 20.07 ? 274  LEU B N     1 
ATOM   5271  C  CA    . LEU J  3 274 ? 42.608  51.423  119.220 1.00 19.95 ? 274  LEU B CA    1 
ATOM   5272  C  C     . LEU J  3 274 ? 41.666  50.255  118.944 1.00 17.16 ? 274  LEU B C     1 
ATOM   5273  O  O     . LEU J  3 274 ? 41.784  49.581  117.905 1.00 21.46 ? 274  LEU B O     1 
ATOM   5274  C  CB    . LEU J  3 274 ? 42.272  52.607  118.285 1.00 20.20 ? 274  LEU B CB    1 
ATOM   5275  C  CG    . LEU J  3 274 ? 40.871  53.208  118.390 1.00 19.90 ? 274  LEU B CG    1 
ATOM   5276  C  CD1   . LEU J  3 274 ? 40.711  53.948  119.716 1.00 22.04 ? 274  LEU B CD1   1 
ATOM   5277  C  CD2   . LEU J  3 274 ? 40.657  54.197  117.222 1.00 23.35 ? 274  LEU B CD2   1 
ATOM   5278  N  N     . LYS J  3 275 ? 40.760  49.994  119.868 1.00 17.59 ? 275  LYS B N     1 
ATOM   5279  C  CA    . LYS J  3 275 ? 39.757  48.935  119.731 1.00 19.53 ? 275  LYS B CA    1 
ATOM   5280  C  C     . LYS J  3 275 ? 38.383  49.472  120.138 1.00 21.34 ? 275  LYS B C     1 
ATOM   5281  O  O     . LYS J  3 275 ? 38.225  50.666  120.432 1.00 23.10 ? 275  LYS B O     1 
ATOM   5282  C  CB    . LYS J  3 275 ? 40.115  47.731  120.617 1.00 20.42 ? 275  LYS B CB    1 
ATOM   5283  C  CG    . LYS J  3 275 ? 41.482  47.144  120.311 1.00 17.82 ? 275  LYS B CG    1 
ATOM   5284  C  CD    . LYS J  3 275 ? 41.770  45.923  121.220 1.00 17.62 ? 275  LYS B CD    1 
ATOM   5285  C  CE    . LYS J  3 275 ? 43.139  45.326  120.934 1.00 19.81 ? 275  LYS B CE    1 
ATOM   5286  N  NZ    . LYS J  3 275 ? 43.299  44.000  121.634 1.00 22.65 ? 275  LYS B NZ    1 
ATOM   5287  N  N     . ASP J  3 276 ? 37.386  48.591  120.175 1.00 20.41 ? 276  ASP B N     1 
ATOM   5288  C  CA    . ASP J  3 276 ? 36.039  48.980  120.576 1.00 21.27 ? 276  ASP B CA    1 
ATOM   5289  C  C     . ASP J  3 276 ? 35.844  48.758  122.070 1.00 23.26 ? 276  ASP B C     1 
ATOM   5290  O  O     . ASP J  3 276 ? 36.555  47.951  122.685 1.00 21.36 ? 276  ASP B O     1 
ATOM   5291  C  CB    . ASP J  3 276 ? 34.996  48.144  119.823 1.00 22.01 ? 276  ASP B CB    1 
ATOM   5292  C  CG    . ASP J  3 276 ? 33.577  48.591  120.113 1.00 19.41 ? 276  ASP B CG    1 
ATOM   5293  O  OD1   . ASP J  3 276 ? 33.236  49.746  119.733 1.00 23.49 ? 276  ASP B OD1   1 
ATOM   5294  O  OD2   . ASP J  3 276 ? 32.789  47.802  120.709 1.00 22.01 ? 276  ASP B OD2   1 
ATOM   5295  N  N     . ILE J  3 277 ? 34.873  49.450  122.657 1.00 21.32 ? 277  ILE B N     1 
ATOM   5296  C  CA    . ILE J  3 277 ? 34.575  49.265  124.075 1.00 21.65 ? 277  ILE B CA    1 
ATOM   5297  C  C     . ILE J  3 277 ? 34.260  47.773  124.349 1.00 24.79 ? 277  ILE B C     1 
ATOM   5298  O  O     . ILE J  3 277 ? 34.577  47.237  125.427 1.00 22.69 ? 277  ILE B O     1 
ATOM   5299  C  CB    . ILE J  3 277 ? 33.372  50.165  124.502 1.00 20.82 ? 277  ILE B CB    1 
ATOM   5300  C  CG1   . ILE J  3 277 ? 33.050  49.971  125.980 1.00 22.59 ? 277  ILE B CG1   1 
ATOM   5301  C  CG2   . ILE J  3 277 ? 32.128  49.870  123.629 1.00 24.13 ? 277  ILE B CG2   1 
ATOM   5302  C  CD1   . ILE J  3 277 ? 34.180  50.429  126.892 1.00 20.89 ? 277  ILE B CD1   1 
ATOM   5303  N  N     . SER J  3 278 ? 33.685  47.084  123.359 1.00 21.63 ? 278  SER B N     1 
ATOM   5304  C  CA    . SER J  3 278 ? 33.337  45.676  123.542 1.00 22.39 ? 278  SER B CA    1 
ATOM   5305  C  C     . SER J  3 278 ? 34.544  44.767  123.644 1.00 20.71 ? 278  SER B C     1 
ATOM   5306  O  O     . SER J  3 278 ? 34.407  43.635  124.088 1.00 22.79 ? 278  SER B O     1 
ATOM   5307  C  CB    . SER J  3 278 ? 32.414  45.176  122.418 1.00 19.86 ? 278  SER B CB    1 
ATOM   5308  O  OG    . SER J  3 278 ? 33.109  45.062  121.194 1.00 23.41 ? 278  SER B OG    1 
ATOM   5309  N  N     . ASP J  3 279 ? 35.714  45.247  123.219 1.00 19.48 ? 279  ASP B N     1 
ATOM   5310  C  CA    . ASP J  3 279 ? 36.945  44.446  123.309 1.00 20.72 ? 279  ASP B CA    1 
ATOM   5311  C  C     . ASP J  3 279 ? 37.573  44.493  124.697 1.00 21.64 ? 279  ASP B C     1 
ATOM   5312  O  O     . ASP J  3 279 ? 38.339  43.587  125.057 1.00 21.05 ? 279  ASP B O     1 
ATOM   5313  C  CB    . ASP J  3 279 ? 37.997  44.932  122.314 1.00 21.08 ? 279  ASP B CB    1 
ATOM   5314  C  CG    . ASP J  3 279 ? 37.583  44.713  120.871 1.00 24.37 ? 279  ASP B CG    1 
ATOM   5315  O  OD1   . ASP J  3 279 ? 37.385  43.547  120.500 1.00 22.71 ? 279  ASP B OD1   1 
ATOM   5316  O  OD2   . ASP J  3 279 ? 37.472  45.699  120.114 1.00 20.92 ? 279  ASP B OD2   1 
ATOM   5317  N  N     . LEU J  3 280 ? 37.239  45.516  125.481 1.00 18.66 ? 280  LEU B N     1 
ATOM   5318  C  CA    . LEU J  3 280 ? 37.851  45.676  126.811 1.00 19.81 ? 280  LEU B CA    1 
ATOM   5319  C  C     . LEU J  3 280 ? 37.665  44.541  127.828 1.00 20.16 ? 280  LEU B C     1 
ATOM   5320  O  O     . LEU J  3 280 ? 38.654  44.091  128.412 1.00 18.90 ? 280  LEU B O     1 
ATOM   5321  C  CB    . LEU J  3 280 ? 37.419  47.014  127.438 1.00 19.53 ? 280  LEU B CB    1 
ATOM   5322  C  CG    . LEU J  3 280 ? 38.070  47.335  128.784 1.00 19.76 ? 280  LEU B CG    1 
ATOM   5323  C  CD1   . LEU J  3 280 ? 39.585  47.253  128.673 1.00 20.43 ? 280  LEU B CD1   1 
ATOM   5324  C  CD2   . LEU J  3 280 ? 37.625  48.744  129.228 1.00 19.87 ? 280  LEU B CD2   1 
ATOM   5325  N  N     . PRO J  3 281 ? 36.424  44.044  128.046 1.00 20.69 ? 281  PRO B N     1 
ATOM   5326  C  CA    . PRO J  3 281 ? 36.261  42.957  129.032 1.00 18.53 ? 281  PRO B CA    1 
ATOM   5327  C  C     . PRO J  3 281 ? 37.136  41.744  128.726 1.00 19.09 ? 281  PRO B C     1 
ATOM   5328  O  O     . PRO J  3 281 ? 37.791  41.200  129.624 1.00 21.53 ? 281  PRO B O     1 
ATOM   5329  C  CB    . PRO J  3 281 ? 34.767  42.641  128.957 1.00 22.52 ? 281  PRO B CB    1 
ATOM   5330  C  CG    . PRO J  3 281 ? 34.159  43.948  128.563 1.00 21.40 ? 281  PRO B CG    1 
ATOM   5331  C  CD    . PRO J  3 281 ? 35.107  44.456  127.508 1.00 20.33 ? 281  PRO B CD    1 
ATOM   5332  N  N     . LEU J  3 282 ? 37.162  41.309  127.468 1.00 19.48 ? 282  LEU B N     1 
ATOM   5333  C  CA    . LEU J  3 282 ? 38.009  40.176  127.115 1.00 21.62 ? 282  LEU B CA    1 
ATOM   5334  C  C     . LEU J  3 282 ? 39.491  40.517  127.214 1.00 18.52 ? 282  LEU B C     1 
ATOM   5335  O  O     . LEU J  3 282 ? 40.305  39.663  127.560 1.00 20.01 ? 282  LEU B O     1 
ATOM   5336  C  CB    . LEU J  3 282 ? 37.696  39.671  125.708 1.00 23.06 ? 282  LEU B CB    1 
ATOM   5337  C  CG    . LEU J  3 282 ? 36.575  38.638  125.624 1.00 25.53 ? 282  LEU B CG    1 
ATOM   5338  C  CD1   . LEU J  3 282 ? 36.219  38.428  124.155 1.00 26.49 ? 282  LEU B CD1   1 
ATOM   5339  C  CD2   . LEU J  3 282 ? 37.018  37.332  126.271 1.00 24.47 ? 282  LEU B CD2   1 
ATOM   5340  N  N     . ASP J  3 283 ? 39.859  41.755  126.890 1.00 18.17 ? 283  ASP B N     1 
ATOM   5341  C  CA    . ASP J  3 283 ? 41.259  42.117  126.980 1.00 17.07 ? 283  ASP B CA    1 
ATOM   5342  C  C     . ASP J  3 283 ? 41.699  42.108  128.441 1.00 16.55 ? 283  ASP B C     1 
ATOM   5343  O  O     . ASP J  3 283 ? 42.873  41.884  128.724 1.00 18.36 ? 283  ASP B O     1 
ATOM   5344  C  CB    . ASP J  3 283 ? 41.517  43.475  126.327 1.00 18.56 ? 283  ASP B CB    1 
ATOM   5345  C  CG    . ASP J  3 283 ? 41.670  43.363  124.818 1.00 21.15 ? 283  ASP B CG    1 
ATOM   5346  O  OD1   . ASP J  3 283 ? 41.632  42.224  124.295 1.00 23.19 ? 283  ASP B OD1   1 
ATOM   5347  O  OD2   . ASP J  3 283 ? 41.838  44.401  124.156 1.00 19.45 ? 283  ASP B OD2   1 
ATOM   5348  N  N     . LEU J  3 284 ? 40.761  42.330  129.355 1.00 15.80 ? 284  LEU B N     1 
ATOM   5349  C  CA    . LEU J  3 284 ? 41.079  42.302  130.782 1.00 18.02 ? 284  LEU B CA    1 
ATOM   5350  C  C     . LEU J  3 284 ? 41.209  40.874  131.300 1.00 17.90 ? 284  LEU B C     1 
ATOM   5351  O  O     . LEU J  3 284 ? 41.506  40.671  132.489 1.00 18.92 ? 284  LEU B O     1 
ATOM   5352  C  CB    . LEU J  3 284 ? 39.993  43.033  131.583 1.00 20.04 ? 284  LEU B CB    1 
ATOM   5353  C  CG    . LEU J  3 284 ? 39.851  44.540  131.362 1.00 21.38 ? 284  LEU B CG    1 
ATOM   5354  C  CD1   . LEU J  3 284 ? 38.657  45.051  132.148 1.00 23.36 ? 284  LEU B CD1   1 
ATOM   5355  C  CD2   . LEU J  3 284 ? 41.112  45.251  131.805 1.00 24.43 ? 284  LEU B CD2   1 
ATOM   5356  N  N     . ALA J  3 285 ? 40.966  39.884  130.435 1.00 18.43 ? 285  ALA B N     1 
ATOM   5357  C  CA    . ALA J  3 285 ? 41.037  38.467  130.816 1.00 21.84 ? 285  ALA B CA    1 
ATOM   5358  C  C     . ALA J  3 285 ? 42.322  37.725  130.402 1.00 22.30 ? 285  ALA B C     1 
ATOM   5359  O  O     . ALA J  3 285 ? 42.447  36.518  130.652 1.00 20.51 ? 285  ALA B O     1 
ATOM   5360  C  CB    . ALA J  3 285 ? 39.809  37.711  130.251 1.00 21.42 ? 285  ALA B CB    1 
ATOM   5361  N  N     . VAL J  3 286 ? 43.271  38.418  129.773 1.00 18.99 ? 286  VAL B N     1 
ATOM   5362  C  CA    . VAL J  3 286 ? 44.496  37.756  129.329 1.00 20.57 ? 286  VAL B CA    1 
ATOM   5363  C  C     . VAL J  3 286 ? 45.324  37.169  130.488 1.00 20.79 ? 286  VAL B C     1 
ATOM   5364  O  O     . VAL J  3 286 ? 45.969  36.101  130.290 1.00 19.35 ? 286  VAL B O     1 
ATOM   5365  C  CB    . VAL J  3 286 ? 45.404  38.706  128.477 1.00 22.06 ? 286  VAL B CB    1 
ATOM   5366  C  CG1   . VAL J  3 286 ? 44.625  39.270  127.294 1.00 20.32 ? 286  VAL B CG1   1 
ATOM   5367  C  CG2   . VAL J  3 286 ? 45.955  39.814  129.331 1.00 23.15 ? 286  VAL B CG2   1 
ATOM   5368  O  OXT   . VAL J  3 286 ? 45.332  37.810  131.571 1.00 21.45 ? 286  VAL B OXT   1 
ATOM   5369  N  N     . MET K  3 1   ? 57.955  17.478  154.027 1.00 57.41 ? 1    MET C N     1 
ATOM   5370  C  CA    . MET K  3 1   ? 58.098  17.531  152.547 1.00 56.67 ? 1    MET C CA    1 
ATOM   5371  C  C     . MET K  3 1   ? 56.926  16.792  151.939 1.00 55.27 ? 1    MET C C     1 
ATOM   5372  O  O     . MET K  3 1   ? 57.081  15.742  151.303 1.00 56.18 ? 1    MET C O     1 
ATOM   5373  C  CB    . MET K  3 1   ? 59.396  16.859  152.117 1.00 58.25 ? 1    MET C CB    1 
ATOM   5374  C  CG    . MET K  3 1   ? 60.089  17.563  150.982 1.00 60.04 ? 1    MET C CG    1 
ATOM   5375  S  SD    . MET K  3 1   ? 61.583  18.336  151.573 1.00 60.04 ? 1    MET C SD    1 
ATOM   5376  C  CE    . MET K  3 1   ? 62.402  18.692  150.025 1.00 60.04 ? 1    MET C CE    1 
ATOM   5377  N  N     . GLN K  3 2   ? 55.749  17.363  152.135 1.00 51.18 ? 2    GLN C N     1 
ATOM   5378  C  CA    . GLN K  3 2   ? 54.546  16.750  151.649 1.00 43.88 ? 2    GLN C CA    1 
ATOM   5379  C  C     . GLN K  3 2   ? 53.892  17.510  150.504 1.00 34.95 ? 2    GLN C C     1 
ATOM   5380  O  O     . GLN K  3 2   ? 53.657  16.932  149.450 1.00 35.88 ? 2    GLN C O     1 
ATOM   5381  C  CB    . GLN K  3 2   ? 53.552  16.584  152.815 1.00 47.19 ? 2    GLN C CB    1 
ATOM   5382  C  CG    . GLN K  3 2   ? 52.465  15.572  152.549 1.00 48.71 ? 2    GLN C CG    1 
ATOM   5383  C  CD    . GLN K  3 2   ? 53.015  14.161  152.386 1.00 52.01 ? 2    GLN C CD    1 
ATOM   5384  O  OE1   . GLN K  3 2   ? 53.487  13.550  153.346 1.00 53.59 ? 2    GLN C OE1   1 
ATOM   5385  N  NE2   . GLN K  3 2   ? 52.959  13.640  151.169 1.00 51.90 ? 2    GLN C NE2   1 
ATOM   5386  N  N     . PRO K  3 3   ? 53.616  18.818  150.680 1.00 32.20 ? 3    PRO C N     1 
ATOM   5387  C  CA    . PRO K  3 3   ? 52.969  19.539  149.574 1.00 26.38 ? 3    PRO C CA    1 
ATOM   5388  C  C     . PRO K  3 3   ? 53.743  19.459  148.262 1.00 24.88 ? 3    PRO C C     1 
ATOM   5389  O  O     . PRO K  3 3   ? 54.976  19.468  148.247 1.00 22.47 ? 3    PRO C O     1 
ATOM   5390  C  CB    . PRO K  3 3   ? 52.809  20.960  150.121 1.00 26.32 ? 3    PRO C CB    1 
ATOM   5391  C  CG    . PRO K  3 3   ? 53.935  21.096  151.081 1.00 30.33 ? 3    PRO C CG    1 
ATOM   5392  C  CD    . PRO K  3 3   ? 54.037  19.747  151.746 1.00 27.54 ? 3    PRO C CD    1 
ATOM   5393  N  N     . LEU K  3 4   ? 52.996  19.379  147.164 1.00 23.54 ? 4    LEU C N     1 
ATOM   5394  C  CA    . LEU K  3 4   ? 53.591  19.230  145.848 1.00 21.25 ? 4    LEU C CA    1 
ATOM   5395  C  C     . LEU K  3 4   ? 54.581  20.320  145.447 1.00 21.71 ? 4    LEU C C     1 
ATOM   5396  O  O     . LEU K  3 4   ? 55.530  20.029  144.738 1.00 21.75 ? 4    LEU C O     1 
ATOM   5397  C  CB    . LEU K  3 4   ? 52.505  19.115  144.774 1.00 24.25 ? 4    LEU C CB    1 
ATOM   5398  C  CG    . LEU K  3 4   ? 51.616  17.869  144.891 1.00 28.05 ? 4    LEU C CG    1 
ATOM   5399  C  CD1   . LEU K  3 4   ? 50.730  17.735  143.643 1.00 30.73 ? 4    LEU C CD1   1 
ATOM   5400  C  CD2   . LEU K  3 4   ? 52.495  16.632  145.042 1.00 32.50 ? 4    LEU C CD2   1 
ATOM   5401  N  N     . PHE K  3 5   ? 54.375  21.557  145.875 1.00 21.04 ? 5    PHE C N     1 
ATOM   5402  C  CA    . PHE K  3 5   ? 55.340  22.597  145.485 1.00 20.81 ? 5    PHE C CA    1 
ATOM   5403  C  C     . PHE K  3 5   ? 56.649  22.392  146.210 1.00 21.84 ? 5    PHE C C     1 
ATOM   5404  O  O     . PHE K  3 5   ? 57.710  22.769  145.712 1.00 19.43 ? 5    PHE C O     1 
ATOM   5405  C  CB    . PHE K  3 5   ? 54.789  23.999  145.744 1.00 17.04 ? 5    PHE C CB    1 
ATOM   5406  C  CG    . PHE K  3 5   ? 53.843  24.490  144.663 1.00 21.93 ? 5    PHE C CG    1 
ATOM   5407  C  CD1   . PHE K  3 5   ? 53.328  25.781  144.702 1.00 27.98 ? 5    PHE C CD1   1 
ATOM   5408  C  CD2   . PHE K  3 5   ? 53.481  23.660  143.612 1.00 21.68 ? 5    PHE C CD2   1 
ATOM   5409  C  CE1   . PHE K  3 5   ? 52.467  26.242  143.697 1.00 30.86 ? 5    PHE C CE1   1 
ATOM   5410  C  CE2   . PHE K  3 5   ? 52.626  24.105  142.604 1.00 24.65 ? 5    PHE C CE2   1 
ATOM   5411  C  CZ    . PHE K  3 5   ? 52.118  25.401  142.647 1.00 23.46 ? 5    PHE C CZ    1 
ATOM   5412  N  N     . THR K  3 6   ? 56.578  21.759  147.379 1.00 18.97 ? 6    THR C N     1 
ATOM   5413  C  CA    . THR K  3 6   ? 57.784  21.469  148.145 1.00 21.29 ? 6    THR C CA    1 
ATOM   5414  C  C     . THR K  3 6   ? 58.511  20.349  147.439 1.00 19.57 ? 6    THR C C     1 
ATOM   5415  O  O     . THR K  3 6   ? 59.734  20.398  147.304 1.00 19.85 ? 6    THR C O     1 
ATOM   5416  C  CB    . THR K  3 6   ? 57.432  21.067  149.578 1.00 20.47 ? 6    THR C CB    1 
ATOM   5417  O  OG1   . THR K  3 6   ? 56.783  22.171  150.198 1.00 22.36 ? 6    THR C OG1   1 
ATOM   5418  C  CG2   . THR K  3 6   ? 58.694  20.714  150.389 1.00 22.38 ? 6    THR C CG2   1 
ATOM   5419  N  N     . GLN K  3 7   ? 57.757  19.354  146.960 1.00 19.98 ? 7    GLN C N     1 
ATOM   5420  C  CA    . GLN K  3 7   ? 58.337  18.245  146.225 1.00 22.54 ? 7    GLN C CA    1 
ATOM   5421  C  C     . GLN K  3 7   ? 58.975  18.767  144.918 1.00 21.73 ? 7    GLN C C     1 
ATOM   5422  O  O     . GLN K  3 7   ? 60.069  18.347  144.534 1.00 21.99 ? 7    GLN C O     1 
ATOM   5423  C  CB    . GLN K  3 7   ? 57.259  17.197  145.923 1.00 23.47 ? 7    GLN C CB    1 
ATOM   5424  C  CG    . GLN K  3 7   ? 56.760  16.469  147.181 1.00 26.21 ? 7    GLN C CG    1 
ATOM   5425  C  CD    . GLN K  3 7   ? 55.760  15.373  146.850 1.00 26.83 ? 7    GLN C CD    1 
ATOM   5426  O  OE1   . GLN K  3 7   ? 55.974  14.589  145.927 1.00 31.45 ? 7    GLN C OE1   1 
ATOM   5427  N  NE2   . GLN K  3 7   ? 54.665  15.313  147.604 1.00 29.90 ? 7    GLN C NE2   1 
ATOM   5428  N  N     . GLU K  3 8   ? 58.295  19.698  144.253 1.00 21.03 ? 8    GLU C N     1 
ATOM   5429  C  CA    . GLU K  3 8   ? 58.835  20.260  143.006 1.00 20.13 ? 8    GLU C CA    1 
ATOM   5430  C  C     . GLU K  3 8   ? 60.124  21.037  143.267 1.00 18.11 ? 8    GLU C C     1 
ATOM   5431  O  O     . GLU K  3 8   ? 61.063  20.989  142.483 1.00 20.28 ? 8    GLU C O     1 
ATOM   5432  C  CB    . GLU K  3 8   ? 57.805  21.190  142.354 1.00 22.13 ? 8    GLU C CB    1 
ATOM   5433  C  CG    . GLU K  3 8   ? 56.578  20.456  141.850 1.00 34.11 ? 8    GLU C CG    1 
ATOM   5434  C  CD    . GLU K  3 8   ? 56.743  19.884  140.459 1.00 40.43 ? 8    GLU C CD    1 
ATOM   5435  O  OE1   . GLU K  3 8   ? 57.873  19.497  140.066 1.00 41.22 ? 8    GLU C OE1   1 
ATOM   5436  O  OE2   . GLU K  3 8   ? 55.712  19.810  139.758 1.00 45.69 ? 8    GLU C OE2   1 
ATOM   5437  N  N     . ARG K  3 9   ? 60.155  21.778  144.359 1.00 16.78 ? 9    ARG C N     1 
ATOM   5438  C  CA    . ARG K  3 9   ? 61.351  22.536  144.714 1.00 15.89 ? 9    ARG C CA    1 
ATOM   5439  C  C     . ARG K  3 9   ? 62.515  21.571  144.930 1.00 19.22 ? 9    ARG C C     1 
ATOM   5440  O  O     . ARG K  3 9   ? 63.658  21.840  144.526 1.00 17.60 ? 9    ARG C O     1 
ATOM   5441  C  CB    . ARG K  3 9   ? 61.084  23.336  145.991 1.00 16.73 ? 9    ARG C CB    1 
ATOM   5442  C  CG    . ARG K  3 9   ? 62.188  24.299  146.386 1.00 18.80 ? 9    ARG C CG    1 
ATOM   5443  C  CD    . ARG K  3 9   ? 61.797  25.062  147.646 1.00 18.05 ? 9    ARG C CD    1 
ATOM   5444  N  NE    . ARG K  3 9   ? 62.683  26.176  147.985 1.00 17.29 ? 9    ARG C NE    1 
ATOM   5445  C  CZ    . ARG K  3 9   ? 63.762  26.096  148.766 1.00 19.38 ? 9    ARG C CZ    1 
ATOM   5446  N  NH1   . ARG K  3 9   ? 64.124  24.926  149.311 1.00 18.86 ? 9    ARG C NH1   1 
ATOM   5447  N  NH2   . ARG K  3 9   ? 64.451  27.195  149.046 1.00 16.11 ? 9    ARG C NH2   1 
ATOM   5448  N  N     . ARG K  3 10  ? 62.242  20.439  145.586 1.00 18.64 ? 10   ARG C N     1 
ATOM   5449  C  CA    . ARG K  3 10  ? 63.310  19.465  145.827 1.00 20.35 ? 10   ARG C CA    1 
ATOM   5450  C  C     . ARG K  3 10  ? 63.802  18.822  144.527 1.00 21.31 ? 10   ARG C C     1 
ATOM   5451  O  O     . ARG K  3 10  ? 65.004  18.576  144.381 1.00 23.05 ? 10   ARG C O     1 
ATOM   5452  C  CB    . ARG K  3 10  ? 62.850  18.364  146.806 1.00 23.05 ? 10   ARG C CB    1 
ATOM   5453  C  CG    . ARG K  3 10  ? 63.990  17.392  147.158 1.00 31.33 ? 10   ARG C CG    1 
ATOM   5454  C  CD    . ARG K  3 10  ? 65.285  18.121  147.559 1.00 37.32 ? 10   ARG C CD    1 
ATOM   5455  N  NE    . ARG K  3 10  ? 66.361  17.186  147.883 1.00 46.10 ? 10   ARG C NE    1 
ATOM   5456  C  CZ    . ARG K  3 10  ? 67.609  17.544  148.178 1.00 47.17 ? 10   ARG C CZ    1 
ATOM   5457  N  NH1   . ARG K  3 10  ? 67.951  18.828  148.192 1.00 43.01 ? 10   ARG C NH1   1 
ATOM   5458  N  NH2   . ARG K  3 10  ? 68.520  16.615  148.459 1.00 48.40 ? 10   ARG C NH2   1 
ATOM   5459  N  N     . ILE K  3 11  ? 62.879  18.553  143.607 1.00 20.88 ? 11   ILE C N     1 
ATOM   5460  C  CA    . ILE K  3 11  ? 63.209  17.975  142.305 1.00 18.35 ? 11   ILE C CA    1 
ATOM   5461  C  C     . ILE K  3 11  ? 64.128  18.966  141.562 1.00 20.44 ? 11   ILE C C     1 
ATOM   5462  O  O     . ILE K  3 11  ? 65.132  18.570  140.965 1.00 19.55 ? 11   ILE C O     1 
ATOM   5463  C  CB    . ILE K  3 11  ? 61.921  17.688  141.481 1.00 20.75 ? 11   ILE C CB    1 
ATOM   5464  C  CG1   . ILE K  3 11  ? 61.201  16.447  142.032 1.00 24.36 ? 11   ILE C CG1   1 
ATOM   5465  C  CG2   . ILE K  3 11  ? 62.278  17.495  140.018 1.00 24.46 ? 11   ILE C CG2   1 
ATOM   5466  C  CD1   . ILE K  3 11  ? 59.853  16.189  141.426 1.00 24.38 ? 11   ILE C CD1   1 
ATOM   5467  N  N     . PHE K  3 12  ? 63.777  20.248  141.624 1.00 18.19 ? 12   PHE C N     1 
ATOM   5468  C  CA    . PHE K  3 12  ? 64.560  21.338  141.003 1.00 18.68 ? 12   PHE C CA    1 
ATOM   5469  C  C     . PHE K  3 12  ? 66.000  21.304  141.538 1.00 21.06 ? 12   PHE C C     1 
ATOM   5470  O  O     . PHE K  3 12  ? 66.963  21.268  140.759 1.00 18.47 ? 12   PHE C O     1 
ATOM   5471  C  CB    . PHE K  3 12  ? 63.847  22.668  141.321 1.00 16.63 ? 12   PHE C CB    1 
ATOM   5472  C  CG    . PHE K  3 12  ? 64.679  23.916  141.096 1.00 16.87 ? 12   PHE C CG    1 
ATOM   5473  C  CD1   . PHE K  3 12  ? 64.911  24.392  139.813 1.00 17.32 ? 12   PHE C CD1   1 
ATOM   5474  C  CD2   . PHE K  3 12  ? 65.158  24.654  142.181 1.00 18.25 ? 12   PHE C CD2   1 
ATOM   5475  C  CE1   . PHE K  3 12  ? 65.604  25.591  139.615 1.00 17.16 ? 12   PHE C CE1   1 
ATOM   5476  C  CE2   . PHE K  3 12  ? 65.858  25.865  141.995 1.00 17.69 ? 12   PHE C CE2   1 
ATOM   5477  C  CZ    . PHE K  3 12  ? 66.077  26.332  140.703 1.00 18.18 ? 12   PHE C CZ    1 
ATOM   5478  N  N     . HIS K  3 13  ? 66.162  21.281  142.863 1.00 17.23 ? 13   HIS C N     1 
ATOM   5479  C  CA    . HIS K  3 13  ? 67.498  21.220  143.446 1.00 19.90 ? 13   HIS C CA    1 
ATOM   5480  C  C     . HIS K  3 13  ? 68.225  19.936  143.052 1.00 18.29 ? 13   HIS C C     1 
ATOM   5481  O  O     . HIS K  3 13  ? 69.415  19.966  142.769 1.00 19.18 ? 13   HIS C O     1 
ATOM   5482  C  CB    . HIS K  3 13  ? 67.420  21.304  144.976 1.00 19.40 ? 13   HIS C CB    1 
ATOM   5483  C  CG    . HIS K  3 13  ? 67.069  22.669  145.479 1.00 18.60 ? 13   HIS C CG    1 
ATOM   5484  N  ND1   . HIS K  3 13  ? 66.539  22.888  146.731 1.00 22.44 ? 13   HIS C ND1   1 
ATOM   5485  C  CD2   . HIS K  3 13  ? 67.240  23.887  144.921 1.00 20.29 ? 13   HIS C CD2   1 
ATOM   5486  C  CE1   . HIS K  3 13  ? 66.408  24.189  146.928 1.00 21.30 ? 13   HIS C CE1   1 
ATOM   5487  N  NE2   . HIS K  3 13  ? 66.826  24.821  145.845 1.00 18.35 ? 13   HIS C NE2   1 
ATOM   5488  N  N     . LYS K  3 14  ? 67.510  18.807  143.055 1.00 19.01 ? 14   LYS C N     1 
ATOM   5489  C  CA    . LYS K  3 14  ? 68.130  17.536  142.684 1.00 21.55 ? 14   LYS C CA    1 
ATOM   5490  C  C     . LYS K  3 14  ? 68.674  17.527  141.256 1.00 24.13 ? 14   LYS C C     1 
ATOM   5491  O  O     . LYS K  3 14  ? 69.693  16.885  140.973 1.00 23.46 ? 14   LYS C O     1 
ATOM   5492  C  CB    . LYS K  3 14  ? 67.137  16.383  142.892 1.00 23.73 ? 14   LYS C CB    1 
ATOM   5493  C  CG    . LYS K  3 14  ? 67.765  15.017  142.744 1.00 34.72 ? 14   LYS C CG    1 
ATOM   5494  C  CD    . LYS K  3 14  ? 66.977  13.934  143.489 1.00 43.29 ? 14   LYS C CD    1 
ATOM   5495  C  CE    . LYS K  3 14  ? 67.851  12.702  143.701 1.00 49.61 ? 14   LYS C CE    1 
ATOM   5496  N  NZ    . LYS K  3 14  ? 67.123  11.559  144.337 1.00 57.66 ? 14   LYS C NZ    1 
ATOM   5497  N  N     . LYS K  3 15  ? 67.988  18.218  140.348 1.00 19.31 ? 15   LYS C N     1 
ATOM   5498  C  CA    . LYS K  3 15  ? 68.455  18.291  138.961 1.00 20.04 ? 15   LYS C CA    1 
ATOM   5499  C  C     . LYS K  3 15  ? 69.772  19.054  138.907 1.00 19.19 ? 15   LYS C C     1 
ATOM   5500  O  O     . LYS K  3 15  ? 70.676  18.720  138.124 1.00 19.79 ? 15   LYS C O     1 
ATOM   5501  C  CB    . LYS K  3 15  ? 67.408  18.997  138.097 1.00 18.42 ? 15   LYS C CB    1 
ATOM   5502  C  CG    . LYS K  3 15  ? 66.144  18.160  137.915 1.00 20.53 ? 15   LYS C CG    1 
ATOM   5503  C  CD    . LYS K  3 15  ? 65.205  18.775  136.886 1.00 22.77 ? 15   LYS C CD    1 
ATOM   5504  C  CE    . LYS K  3 15  ? 64.008  17.852  136.629 1.00 30.15 ? 15   LYS C CE    1 
ATOM   5505  N  NZ    . LYS K  3 15  ? 62.951  18.540  135.837 1.00 28.85 ? 15   LYS C NZ    1 
ATOM   5506  N  N     . LEU K  3 16  ? 69.884  20.081  139.740 1.00 16.67 ? 16   LEU C N     1 
ATOM   5507  C  CA    . LEU K  3 16  ? 71.111  20.866  139.768 1.00 18.20 ? 16   LEU C CA    1 
ATOM   5508  C  C     . LEU K  3 16  ? 72.268  20.051  140.327 1.00 20.96 ? 16   LEU C C     1 
ATOM   5509  O  O     . LEU K  3 16  ? 73.402  20.205  139.896 1.00 20.57 ? 16   LEU C O     1 
ATOM   5510  C  CB    . LEU K  3 16  ? 70.931  22.132  140.597 1.00 18.11 ? 16   LEU C CB    1 
ATOM   5511  C  CG    . LEU K  3 16  ? 69.894  23.144  140.077 1.00 17.48 ? 16   LEU C CG    1 
ATOM   5512  C  CD1   . LEU K  3 16  ? 69.682  24.225  141.129 1.00 18.02 ? 16   LEU C CD1   1 
ATOM   5513  C  CD2   . LEU K  3 16  ? 70.358  23.770  138.770 1.00 18.12 ? 16   LEU C CD2   1 
ATOM   5514  N  N     . LEU K  3 17  ? 71.975  19.185  141.287 1.00 21.16 ? 17   LEU C N     1 
ATOM   5515  C  CA    . LEU K  3 17  ? 73.018  18.352  141.877 1.00 22.66 ? 17   LEU C CA    1 
ATOM   5516  C  C     . LEU K  3 17  ? 73.389  17.219  140.917 1.00 22.48 ? 17   LEU C C     1 
ATOM   5517  O  O     . LEU K  3 17  ? 74.576  16.981  140.651 1.00 23.97 ? 17   LEU C O     1 
ATOM   5518  C  CB    . LEU K  3 17  ? 72.526  17.784  143.215 1.00 22.74 ? 17   LEU C CB    1 
ATOM   5519  C  CG    . LEU K  3 17  ? 72.269  18.833  144.303 1.00 23.34 ? 17   LEU C CG    1 
ATOM   5520  C  CD1   . LEU K  3 17  ? 71.739  18.136  145.568 1.00 28.09 ? 17   LEU C CD1   1 
ATOM   5521  C  CD2   . LEU K  3 17  ? 73.542  19.567  144.617 1.00 23.45 ? 17   LEU C CD2   1 
ATOM   5522  N  N     . ASP K  3 18  ? 72.382  16.534  140.386 1.00 23.92 ? 18   ASP C N     1 
ATOM   5523  C  CA    . ASP K  3 18  ? 72.626  15.412  139.489 1.00 22.42 ? 18   ASP C CA    1 
ATOM   5524  C  C     . ASP K  3 18  ? 73.389  15.773  138.221 1.00 26.16 ? 18   ASP C C     1 
ATOM   5525  O  O     . ASP K  3 18  ? 74.133  14.935  137.687 1.00 28.56 ? 18   ASP C O     1 
ATOM   5526  C  CB    . ASP K  3 18  ? 71.307  14.735  139.109 1.00 24.60 ? 18   ASP C CB    1 
ATOM   5527  C  CG    . ASP K  3 18  ? 70.672  13.988  140.272 1.00 25.24 ? 18   ASP C CG    1 
ATOM   5528  O  OD1   . ASP K  3 18  ? 71.326  13.860  141.330 1.00 29.82 ? 18   ASP C OD1   1 
ATOM   5529  O  OD2   . ASP K  3 18  ? 69.526  13.527  140.116 1.00 30.87 ? 18   ASP C OD2   1 
ATOM   5530  N  N     . GLY K  3 19  ? 73.203  17.004  137.738 1.00 24.08 ? 19   GLY C N     1 
ATOM   5531  C  CA    . GLY K  3 19  ? 73.890  17.445  136.530 1.00 24.66 ? 19   GLY C CA    1 
ATOM   5532  C  C     . GLY K  3 19  ? 75.242  18.069  136.846 1.00 24.86 ? 19   GLY C C     1 
ATOM   5533  O  O     . GLY K  3 19  ? 75.947  18.572  135.957 1.00 26.36 ? 19   GLY C O     1 
ATOM   5534  N  N     . ASN K  3 20  ? 75.611  18.049  138.120 1.00 22.99 ? 20   ASN C N     1 
ATOM   5535  C  CA    . ASN K  3 20  ? 76.871  18.628  138.554 1.00 23.24 ? 20   ASN C CA    1 
ATOM   5536  C  C     . ASN K  3 20  ? 76.900  20.147  138.322 1.00 22.52 ? 20   ASN C C     1 
ATOM   5537  O  O     . ASN K  3 20  ? 77.972  20.755  138.278 1.00 25.01 ? 20   ASN C O     1 
ATOM   5538  C  CB    . ASN K  3 20  ? 78.048  17.940  137.838 1.00 27.45 ? 20   ASN C CB    1 
ATOM   5539  C  CG    . ASN K  3 20  ? 78.295  16.512  138.344 1.00 33.45 ? 20   ASN C CG    1 
ATOM   5540  O  OD1   . ASN K  3 20  ? 79.077  15.754  137.762 1.00 40.16 ? 20   ASN C OD1   1 
ATOM   5541  N  ND2   . ASN K  3 20  ? 77.635  16.152  139.432 1.00 36.25 ? 20   ASN C ND2   1 
ATOM   5542  N  N     . ILE K  3 21  ? 75.718  20.764  138.201 1.00 20.64 ? 21   ILE C N     1 
ATOM   5543  C  CA    . ILE K  3 21  ? 75.643  22.219  138.015 1.00 22.38 ? 21   ILE C CA    1 
ATOM   5544  C  C     . ILE K  3 21  ? 76.023  22.856  139.346 1.00 19.64 ? 21   ILE C C     1 
ATOM   5545  O  O     . ILE K  3 21  ? 76.754  23.851  139.384 1.00 19.27 ? 21   ILE C O     1 
ATOM   5546  C  CB    . ILE K  3 21  ? 74.223  22.701  137.657 1.00 20.88 ? 21   ILE C CB    1 
ATOM   5547  C  CG1   . ILE K  3 21  ? 73.654  21.865  136.511 1.00 26.71 ? 21   ILE C CG1   1 
ATOM   5548  C  CG2   . ILE K  3 21  ? 74.262  24.192  137.271 1.00 19.10 ? 21   ILE C CG2   1 
ATOM   5549  C  CD1   . ILE K  3 21  ? 74.573  21.741  135.357 1.00 29.01 ? 21   ILE C CD1   1 
ATOM   5550  N  N     . LEU K  3 22  ? 75.463  22.309  140.430 1.00 18.75 ? 22   LEU C N     1 
ATOM   5551  C  CA    . LEU K  3 22  ? 75.770  22.763  141.779 1.00 15.99 ? 22   LEU C CA    1 
ATOM   5552  C  C     . LEU K  3 22  ? 76.647  21.647  142.358 1.00 18.45 ? 22   LEU C C     1 
ATOM   5553  O  O     . LEU K  3 22  ? 76.164  20.523  142.567 1.00 19.80 ? 22   LEU C O     1 
ATOM   5554  C  CB    . LEU K  3 22  ? 74.512  22.900  142.642 1.00 18.56 ? 22   LEU C CB    1 
ATOM   5555  C  CG    . LEU K  3 22  ? 74.767  23.446  144.068 1.00 20.78 ? 22   LEU C CG    1 
ATOM   5556  C  CD1   . LEU K  3 22  ? 75.286  24.883  144.035 1.00 22.29 ? 22   LEU C CD1   1 
ATOM   5557  C  CD2   . LEU K  3 22  ? 73.479  23.391  144.837 1.00 17.99 ? 22   LEU C CD2   1 
ATOM   5558  N  N     . ALA K  3 23  ? 77.920  21.957  142.573 1.00 19.01 ? 23   ALA C N     1 
ATOM   5559  C  CA    . ALA K  3 23  ? 78.886  20.989  143.113 1.00 18.20 ? 23   ALA C CA    1 
ATOM   5560  C  C     . ALA K  3 23  ? 80.011  21.755  143.804 1.00 21.04 ? 23   ALA C C     1 
ATOM   5561  O  O     . ALA K  3 23  ? 80.050  22.980  143.773 1.00 18.77 ? 23   ALA C O     1 
ATOM   5562  C  CB    . ALA K  3 23  ? 79.446  20.113  141.959 1.00 19.49 ? 23   ALA C CB    1 
ATOM   5563  N  N     . THR K  3 24  ? 80.950  21.038  144.434 1.00 18.63 ? 24   THR C N     1 
ATOM   5564  C  CA    . THR K  3 24  ? 82.063  21.690  145.122 1.00 19.54 ? 24   THR C CA    1 
ATOM   5565  C  C     . THR K  3 24  ? 83.338  21.198  144.467 1.00 18.26 ? 24   THR C C     1 
ATOM   5566  O  O     . THR K  3 24  ? 83.494  19.996  144.280 1.00 22.39 ? 24   THR C O     1 
ATOM   5567  C  CB    . THR K  3 24  ? 82.114  21.273  146.620 1.00 20.06 ? 24   THR C CB    1 
ATOM   5568  O  OG1   . THR K  3 24  ? 80.854  21.564  147.236 1.00 23.31 ? 24   THR C OG1   1 
ATOM   5569  C  CG2   . THR K  3 24  ? 83.226  21.996  147.359 1.00 20.44 ? 24   THR C CG2   1 
ATOM   5570  N  N     . ASN K  3 25  ? 84.252  22.101  144.126 1.00 17.50 ? 25   ASN C N     1 
ATOM   5571  C  CA    . ASN K  3 25  ? 85.485  21.665  143.487 1.00 18.45 ? 25   ASN C CA    1 
ATOM   5572  C  C     . ASN K  3 25  ? 86.567  21.271  144.493 1.00 20.01 ? 25   ASN C C     1 
ATOM   5573  O  O     . ASN K  3 25  ? 86.336  21.324  145.706 1.00 20.12 ? 25   ASN C O     1 
ATOM   5574  C  CB    . ASN K  3 25  ? 86.018  22.733  142.496 1.00 20.75 ? 25   ASN C CB    1 
ATOM   5575  C  CG    . ASN K  3 25  ? 86.605  23.985  143.159 1.00 20.64 ? 25   ASN C CG    1 
ATOM   5576  O  OD1   . ASN K  3 25  ? 86.770  24.110  144.384 1.00 18.91 ? 25   ASN C OD1   1 
ATOM   5577  N  ND2   . ASN K  3 25  ? 86.945  24.952  142.302 1.00 25.92 ? 25   ASN C ND2   1 
ATOM   5578  N  N     . ASN K  3 26  ? 87.739  20.901  143.980 1.00 22.67 ? 26   ASN C N     1 
ATOM   5579  C  CA    . ASN K  3 26  ? 88.850  20.475  144.836 1.00 22.46 ? 26   ASN C CA    1 
ATOM   5580  C  C     . ASN K  3 26  ? 89.313  21.507  145.849 1.00 24.21 ? 26   ASN C C     1 
ATOM   5581  O  O     . ASN K  3 26  ? 89.847  21.139  146.904 1.00 25.04 ? 26   ASN C O     1 
ATOM   5582  C  CB    . ASN K  3 26  ? 90.045  20.049  143.980 1.00 28.23 ? 26   ASN C CB    1 
ATOM   5583  C  CG    . ASN K  3 26  ? 89.889  18.658  143.416 1.00 30.09 ? 26   ASN C CG    1 
ATOM   5584  O  OD1   . ASN K  3 26  ? 90.586  18.282  142.477 1.00 36.95 ? 26   ASN C OD1   1 
ATOM   5585  N  ND2   . ASN K  3 26  ? 88.990  17.880  143.994 1.00 25.03 ? 26   ASN C ND2   1 
ATOM   5586  N  N     . ARG K  3 27  ? 89.134  22.791  145.541 1.00 19.58 ? 27   ARG C N     1 
ATOM   5587  C  CA    . ARG K  3 27  ? 89.524  23.872  146.448 1.00 22.14 ? 27   ARG C CA    1 
ATOM   5588  C  C     . ARG K  3 27  ? 88.414  24.248  147.430 1.00 22.15 ? 27   ARG C C     1 
ATOM   5589  O  O     . ARG K  3 27  ? 88.515  25.254  148.142 1.00 23.88 ? 27   ARG C O     1 
ATOM   5590  C  CB    . ARG K  3 27  ? 89.942  25.132  145.660 1.00 25.36 ? 27   ARG C CB    1 
ATOM   5591  C  CG    . ARG K  3 27  ? 91.231  24.975  144.881 1.00 32.04 ? 27   ARG C CG    1 
ATOM   5592  C  CD    . ARG K  3 27  ? 91.753  26.339  144.443 1.00 42.03 ? 27   ARG C CD    1 
ATOM   5593  N  NE    . ARG K  3 27  ? 92.970  26.242  143.633 1.00 48.51 ? 27   ARG C NE    1 
ATOM   5594  C  CZ    . ARG K  3 27  ? 93.759  27.274  143.345 1.00 48.42 ? 27   ARG C CZ    1 
ATOM   5595  N  NH1   . ARG K  3 27  ? 93.461  28.486  143.804 1.00 49.17 ? 27   ARG C NH1   1 
ATOM   5596  N  NH2   . ARG K  3 27  ? 94.847  27.094  142.602 1.00 49.58 ? 27   ARG C NH2   1 
ATOM   5597  N  N     . GLY K  3 28  ? 87.356  23.435  147.471 1.00 19.72 ? 28   GLY C N     1 
ATOM   5598  C  CA    . GLY K  3 28  ? 86.261  23.698  148.392 1.00 20.64 ? 28   GLY C CA    1 
ATOM   5599  C  C     . GLY K  3 28  ? 85.310  24.815  147.992 1.00 20.00 ? 28   GLY C C     1 
ATOM   5600  O  O     . GLY K  3 28  ? 84.480  25.242  148.784 1.00 20.71 ? 28   GLY C O     1 
ATOM   5601  N  N     . VAL K  3 29  ? 85.431  25.273  146.749 1.00 19.11 ? 29   VAL C N     1 
ATOM   5602  C  CA    . VAL K  3 29  ? 84.551  26.336  146.249 1.00 18.90 ? 29   VAL C CA    1 
ATOM   5603  C  C     . VAL K  3 29  ? 83.313  25.728  145.585 1.00 16.75 ? 29   VAL C C     1 
ATOM   5604  O  O     . VAL K  3 29  ? 83.429  24.929  144.653 1.00 18.86 ? 29   VAL C O     1 
ATOM   5605  C  CB    . VAL K  3 29  ? 85.269  27.211  145.178 1.00 17.41 ? 29   VAL C CB    1 
ATOM   5606  C  CG1   . VAL K  3 29  ? 84.375  28.426  144.834 1.00 19.53 ? 29   VAL C CG1   1 
ATOM   5607  C  CG2   . VAL K  3 29  ? 86.621  27.699  145.694 1.00 19.33 ? 29   VAL C CG2   1 
ATOM   5608  N  N     . VAL K  3 30  ? 82.128  26.105  146.060 1.00 19.32 ? 30   VAL C N     1 
ATOM   5609  C  CA    . VAL K  3 30  ? 80.891  25.600  145.473 1.00 17.26 ? 30   VAL C CA    1 
ATOM   5610  C  C     . VAL K  3 30  ? 80.728  26.339  144.140 1.00 15.45 ? 30   VAL C C     1 
ATOM   5611  O  O     . VAL K  3 30  ? 81.141  27.495  144.023 1.00 18.27 ? 30   VAL C O     1 
ATOM   5612  C  CB    . VAL K  3 30  ? 79.705  25.841  146.412 1.00 17.64 ? 30   VAL C CB    1 
ATOM   5613  C  CG1   . VAL K  3 30  ? 78.414  25.317  145.782 1.00 20.04 ? 30   VAL C CG1   1 
ATOM   5614  C  CG2   . VAL K  3 30  ? 79.989  25.123  147.749 1.00 20.82 ? 30   VAL C CG2   1 
ATOM   5615  N  N     . SER K  3 31  ? 80.128  25.666  143.164 1.00 17.42 ? 31   SER C N     1 
ATOM   5616  C  CA    . SER K  3 31  ? 80.015  26.185  141.803 1.00 17.97 ? 31   SER C CA    1 
ATOM   5617  C  C     . SER K  3 31  ? 79.206  27.453  141.539 1.00 20.76 ? 31   SER C C     1 
ATOM   5618  O  O     . SER K  3 31  ? 79.227  27.953  140.414 1.00 18.81 ? 31   SER C O     1 
ATOM   5619  C  CB    . SER K  3 31  ? 79.554  25.055  140.874 1.00 16.49 ? 31   SER C CB    1 
ATOM   5620  O  OG    . SER K  3 31  ? 78.278  24.599  141.249 1.00 17.94 ? 31   SER C OG    1 
ATOM   5621  N  N     . ASN K  3 32  ? 78.497  27.964  142.541 1.00 16.96 ? 32   ASN C N     1 
ATOM   5622  C  CA    . ASN K  3 32  ? 77.781  29.233  142.364 1.00 16.21 ? 32   ASN C CA    1 
ATOM   5623  C  C     . ASN K  3 32  ? 78.460  30.310  143.199 1.00 15.81 ? 32   ASN C C     1 
ATOM   5624  O  O     . ASN K  3 32  ? 77.953  31.431  143.315 1.00 17.78 ? 32   ASN C O     1 
ATOM   5625  C  CB    . ASN K  3 32  ? 76.283  29.134  142.740 1.00 15.43 ? 32   ASN C CB    1 
ATOM   5626  C  CG    . ASN K  3 32  ? 76.048  28.809  144.207 1.00 16.94 ? 32   ASN C CG    1 
ATOM   5627  O  OD1   . ASN K  3 32  ? 76.884  28.181  144.850 1.00 17.48 ? 32   ASN C OD1   1 
ATOM   5628  N  ND2   . ASN K  3 32  ? 74.877  29.202  144.727 1.00 15.99 ? 32   ASN C ND2   1 
ATOM   5629  N  N     . ALA K  3 33  ? 79.635  29.982  143.767 1.00 16.71 ? 33   ALA C N     1 
ATOM   5630  C  CA    . ALA K  3 33  ? 80.380  30.945  144.581 1.00 16.68 ? 33   ALA C CA    1 
ATOM   5631  C  C     . ALA K  3 33  ? 81.548  31.583  143.841 1.00 16.50 ? 33   ALA C C     1 
ATOM   5632  O  O     . ALA K  3 33  ? 82.002  31.075  142.798 1.00 18.78 ? 33   ALA C O     1 
ATOM   5633  C  CB    . ALA K  3 33  ? 80.931  30.262  145.866 1.00 19.75 ? 33   ALA C CB    1 
ATOM   5634  N  N     . ASP K  3 34  ? 82.016  32.679  144.418 1.00 15.49 ? 34   ASP C N     1 
ATOM   5635  C  CA    . ASP K  3 34  ? 83.177  33.438  143.939 1.00 16.85 ? 34   ASP C CA    1 
ATOM   5636  C  C     . ASP K  3 34  ? 84.242  33.131  145.004 1.00 17.50 ? 34   ASP C C     1 
ATOM   5637  O  O     . ASP K  3 34  ? 84.219  33.704  146.106 1.00 17.38 ? 34   ASP C O     1 
ATOM   5638  C  CB    . ASP K  3 34  ? 82.832  34.931  143.902 1.00 17.33 ? 34   ASP C CB    1 
ATOM   5639  C  CG    . ASP K  3 34  ? 84.031  35.822  143.588 1.00 20.02 ? 34   ASP C CG    1 
ATOM   5640  O  OD1   . ASP K  3 34  ? 85.152  35.293  143.342 1.00 20.43 ? 34   ASP C OD1   1 
ATOM   5641  O  OD2   . ASP K  3 34  ? 83.847  37.060  143.611 1.00 21.87 ? 34   ASP C OD2   1 
ATOM   5642  N  N     . GLY K  3 35  ? 85.147  32.212  144.667 1.00 20.13 ? 35   GLY C N     1 
ATOM   5643  C  CA    . GLY K  3 35  ? 86.173  31.785  145.606 1.00 23.85 ? 35   GLY C CA    1 
ATOM   5644  C  C     . GLY K  3 35  ? 87.045  32.852  146.239 1.00 26.20 ? 35   GLY C C     1 
ATOM   5645  O  O     . GLY K  3 35  ? 87.602  32.643  147.310 1.00 29.72 ? 35   GLY C O     1 
ATOM   5646  N  N     . SER K  3 36  ? 87.155  34.010  145.599 1.00 24.28 ? 36   SER C N     1 
ATOM   5647  C  CA    . SER K  3 36  ? 88.003  35.095  146.112 1.00 25.69 ? 36   SER C CA    1 
ATOM   5648  C  C     . SER K  3 36  ? 87.291  35.919  147.170 1.00 28.00 ? 36   SER C C     1 
ATOM   5649  O  O     . SER K  3 36  ? 87.885  36.781  147.817 1.00 27.82 ? 36   SER C O     1 
ATOM   5650  C  CB    . SER K  3 36  ? 88.381  36.028  144.941 1.00 24.17 ? 36   SER C CB    1 
ATOM   5651  O  OG    . SER K  3 36  ? 87.249  36.818  144.574 1.00 27.02 ? 36   SER C OG    1 
ATOM   5652  N  N     . ASN K  3 37  ? 86.008  35.634  147.346 1.00 24.36 ? 37   ASN C N     1 
ATOM   5653  C  CA    . ASN K  3 37  ? 85.128  36.380  148.234 1.00 24.67 ? 37   ASN C CA    1 
ATOM   5654  C  C     . ASN K  3 37  ? 84.785  35.515  149.447 1.00 22.84 ? 37   ASN C C     1 
ATOM   5655  O  O     . ASN K  3 37  ? 84.023  34.564  149.307 1.00 22.18 ? 37   ASN C O     1 
ATOM   5656  C  CB    . ASN K  3 37  ? 83.861  36.685  147.406 1.00 23.57 ? 37   ASN C CB    1 
ATOM   5657  C  CG    . ASN K  3 37  ? 82.859  37.566  148.119 1.00 29.73 ? 37   ASN C CG    1 
ATOM   5658  O  OD1   . ASN K  3 37  ? 82.752  37.554  149.337 1.00 25.90 ? 37   ASN C OD1   1 
ATOM   5659  N  ND2   . ASN K  3 37  ? 82.077  38.326  147.329 1.00 30.14 ? 37   ASN C ND2   1 
ATOM   5660  N  N     . THR K  3 38  ? 85.316  35.849  150.630 1.00 25.03 ? 38   THR C N     1 
ATOM   5661  C  CA    . THR K  3 38  ? 85.044  35.019  151.811 1.00 27.17 ? 38   THR C CA    1 
ATOM   5662  C  C     . THR K  3 38  ? 83.566  34.808  152.090 1.00 23.80 ? 38   THR C C     1 
ATOM   5663  O  O     . THR K  3 38  ? 83.127  33.700  152.423 1.00 23.88 ? 38   THR C O     1 
ATOM   5664  C  CB    . THR K  3 38  ? 85.675  35.612  153.096 1.00 30.07 ? 38   THR C CB    1 
ATOM   5665  O  OG1   . THR K  3 38  ? 87.089  35.733  152.918 1.00 37.20 ? 38   THR C OG1   1 
ATOM   5666  C  CG2   . THR K  3 38  ? 85.416  34.681  154.289 1.00 36.07 ? 38   THR C CG2   1 
ATOM   5667  N  N     . ARG K  3 39  ? 82.779  35.865  151.980 1.00 22.84 ? 39   ARG C N     1 
ATOM   5668  C  CA    . ARG K  3 39  ? 81.362  35.722  152.258 1.00 21.92 ? 39   ARG C CA    1 
ATOM   5669  C  C     . ARG K  3 39  ? 80.687  34.829  151.221 1.00 19.36 ? 39   ARG C C     1 
ATOM   5670  O  O     . ARG K  3 39  ? 79.874  33.959  151.576 1.00 19.17 ? 39   ARG C O     1 
ATOM   5671  C  CB    . ARG K  3 39  ? 80.718  37.106  152.329 1.00 26.89 ? 39   ARG C CB    1 
ATOM   5672  C  CG    . ARG K  3 39  ? 81.370  37.962  153.403 1.00 31.88 ? 39   ARG C CG    1 
ATOM   5673  C  CD    . ARG K  3 39  ? 80.610  39.245  153.663 1.00 32.25 ? 39   ARG C CD    1 
ATOM   5674  N  NE    . ARG K  3 39  ? 80.918  39.713  155.008 1.00 36.81 ? 39   ARG C NE    1 
ATOM   5675  C  CZ    . ARG K  3 39  ? 80.204  40.622  155.652 1.00 38.30 ? 39   ARG C CZ    1 
ATOM   5676  N  NH1   . ARG K  3 39  ? 79.146  41.152  155.054 1.00 41.09 ? 39   ARG C NH1   1 
ATOM   5677  N  NH2   . ARG K  3 39  ? 80.532  40.986  156.886 1.00 34.42 ? 39   ARG C NH2   1 
ATOM   5678  N  N     . SER K  3 40  ? 81.036  35.012  149.945 1.00 17.81 ? 40   SER C N     1 
ATOM   5679  C  CA    . SER K  3 40  ? 80.448  34.186  148.895 1.00 15.33 ? 40   SER C CA    1 
ATOM   5680  C  C     . SER K  3 40  ? 80.759  32.707  149.133 1.00 15.47 ? 40   SER C C     1 
ATOM   5681  O  O     . SER K  3 40  ? 79.876  31.835  149.059 1.00 17.44 ? 40   SER C O     1 
ATOM   5682  C  CB    . SER K  3 40  ? 80.997  34.586  147.516 1.00 15.23 ? 40   SER C CB    1 
ATOM   5683  O  OG    . SER K  3 40  ? 80.352  33.817  146.513 1.00 17.19 ? 40   SER C OG    1 
ATOM   5684  N  N     . PHE K  3 41  ? 82.031  32.445  149.422 1.00 16.23 ? 41   PHE C N     1 
ATOM   5685  C  CA    . PHE K  3 41  ? 82.534  31.096  149.665 1.00 18.42 ? 41   PHE C CA    1 
ATOM   5686  C  C     . PHE K  3 41  ? 81.758  30.422  150.821 1.00 14.97 ? 41   PHE C C     1 
ATOM   5687  O  O     . PHE K  3 41  ? 81.244  29.316  150.670 1.00 18.27 ? 41   PHE C O     1 
ATOM   5688  C  CB    . PHE K  3 41  ? 84.040  31.189  150.010 1.00 17.75 ? 41   PHE C CB    1 
ATOM   5689  C  CG    . PHE K  3 41  ? 84.698  29.855  150.300 1.00 17.75 ? 41   PHE C CG    1 
ATOM   5690  C  CD1   . PHE K  3 41  ? 85.424  29.188  149.326 1.00 19.70 ? 41   PHE C CD1   1 
ATOM   5691  C  CD2   . PHE K  3 41  ? 84.606  29.290  151.584 1.00 22.66 ? 41   PHE C CD2   1 
ATOM   5692  C  CE1   . PHE K  3 41  ? 86.075  27.964  149.610 1.00 21.17 ? 41   PHE C CE1   1 
ATOM   5693  C  CE2   . PHE K  3 41  ? 85.250  28.068  151.881 1.00 21.24 ? 41   PHE C CE2   1 
ATOM   5694  C  CZ    . PHE K  3 41  ? 85.979  27.412  150.901 1.00 21.49 ? 41   PHE C CZ    1 
ATOM   5695  N  N     . ASN K  3 42  ? 81.661  31.114  151.952 1.00 16.85 ? 42   ASN C N     1 
ATOM   5696  C  CA    . ASN K  3 42  ? 80.988  30.537  153.105 1.00 18.92 ? 42   ASN C CA    1 
ATOM   5697  C  C     . ASN K  3 42  ? 79.470  30.425  152.972 1.00 18.58 ? 42   ASN C C     1 
ATOM   5698  O  O     . ASN K  3 42  ? 78.851  29.443  153.410 1.00 18.85 ? 42   ASN C O     1 
ATOM   5699  C  CB    . ASN K  3 42  ? 81.376  31.335  154.342 1.00 19.06 ? 42   ASN C CB    1 
ATOM   5700  C  CG    . ASN K  3 42  ? 82.849  31.136  154.707 1.00 25.29 ? 42   ASN C CG    1 
ATOM   5701  O  OD1   . ASN K  3 42  ? 83.364  30.018  154.630 1.00 28.01 ? 42   ASN C OD1   1 
ATOM   5702  N  ND2   . ASN K  3 42  ? 83.522  32.207  155.089 1.00 27.99 ? 42   ASN C ND2   1 
ATOM   5703  N  N     . ILE K  3 43  ? 78.856  31.428  152.361 1.00 18.40 ? 43   ILE C N     1 
ATOM   5704  C  CA    . ILE K  3 43  ? 77.413  31.364  152.196 1.00 18.58 ? 43   ILE C CA    1 
ATOM   5705  C  C     . ILE K  3 43  ? 77.049  30.212  151.259 1.00 15.34 ? 43   ILE C C     1 
ATOM   5706  O  O     . ILE K  3 43  ? 76.157  29.417  151.545 1.00 18.12 ? 43   ILE C O     1 
ATOM   5707  C  CB    . ILE K  3 43  ? 76.881  32.691  151.634 1.00 17.05 ? 43   ILE C CB    1 
ATOM   5708  C  CG1   . ILE K  3 43  ? 76.982  33.780  152.708 1.00 19.17 ? 43   ILE C CG1   1 
ATOM   5709  C  CG2   . ILE K  3 43  ? 75.429  32.532  151.195 1.00 17.96 ? 43   ILE C CG2   1 
ATOM   5710  C  CD1   . ILE K  3 43  ? 76.811  35.192  152.160 1.00 22.62 ? 43   ILE C CD1   1 
ATOM   5711  N  N     . ALA K  3 44  ? 77.743  30.131  150.121 1.00 16.70 ? 44   ALA C N     1 
ATOM   5712  C  CA    . ALA K  3 44  ? 77.464  29.092  149.139 1.00 17.59 ? 44   ALA C CA    1 
ATOM   5713  C  C     . ALA K  3 44  ? 77.654  27.694  149.705 1.00 16.81 ? 44   ALA C C     1 
ATOM   5714  O  O     . ALA K  3 44  ? 76.884  26.799  149.387 1.00 20.01 ? 44   ALA C O     1 
ATOM   5715  C  CB    . ALA K  3 44  ? 78.352  29.275  147.896 1.00 16.67 ? 44   ALA C CB    1 
ATOM   5716  N  N     . LYS K  3 45  ? 78.696  27.497  150.520 1.00 18.40 ? 45   LYS C N     1 
ATOM   5717  C  CA    . LYS K  3 45  ? 78.908  26.169  151.094 1.00 20.96 ? 45   LYS C CA    1 
ATOM   5718  C  C     . LYS K  3 45  ? 77.799  25.826  152.094 1.00 18.31 ? 45   LYS C C     1 
ATOM   5719  O  O     . LYS K  3 45  ? 77.340  24.690  152.131 1.00 19.81 ? 45   LYS C O     1 
ATOM   5720  C  CB    . LYS K  3 45  ? 80.287  26.059  151.767 1.00 23.92 ? 45   LYS C CB    1 
ATOM   5721  C  CG    . LYS K  3 45  ? 80.599  24.608  152.188 1.00 27.05 ? 45   LYS C CG    1 
ATOM   5722  C  CD    . LYS K  3 45  ? 80.507  23.646  150.981 1.00 33.46 ? 45   LYS C CD    1 
ATOM   5723  C  CE    . LYS K  3 45  ? 80.835  22.198  151.354 1.00 37.99 ? 45   LYS C CE    1 
ATOM   5724  N  NZ    . LYS K  3 45  ? 80.682  21.224  150.216 1.00 32.82 ? 45   LYS C NZ    1 
ATOM   5725  N  N     . GLY K  3 46  ? 77.387  26.806  152.894 1.00 17.71 ? 46   GLY C N     1 
ATOM   5726  C  CA    . GLY K  3 46  ? 76.291  26.599  153.838 1.00 19.69 ? 46   GLY C CA    1 
ATOM   5727  C  C     . GLY K  3 46  ? 75.025  26.191  153.100 1.00 19.73 ? 46   GLY C C     1 
ATOM   5728  O  O     . GLY K  3 46  ? 74.324  25.274  153.502 1.00 20.51 ? 46   GLY C O     1 
ATOM   5729  N  N     . ILE K  3 47  ? 74.712  26.873  151.997 1.00 18.99 ? 47   ILE C N     1 
ATOM   5730  C  CA    . ILE K  3 47  ? 73.540  26.505  151.218 1.00 17.74 ? 47   ILE C CA    1 
ATOM   5731  C  C     . ILE K  3 47  ? 73.651  25.086  150.660 1.00 18.54 ? 47   ILE C C     1 
ATOM   5732  O  O     . ILE K  3 47  ? 72.693  24.306  150.726 1.00 18.70 ? 47   ILE C O     1 
ATOM   5733  C  CB    . ILE K  3 47  ? 73.322  27.511  150.017 1.00 16.45 ? 47   ILE C CB    1 
ATOM   5734  C  CG1   . ILE K  3 47  ? 72.916  28.871  150.579 1.00 18.86 ? 47   ILE C CG1   1 
ATOM   5735  C  CG2   . ILE K  3 47  ? 72.256  26.970  149.016 1.00 18.94 ? 47   ILE C CG2   1 
ATOM   5736  C  CD1   . ILE K  3 47  ? 72.811  29.987  149.517 1.00 22.52 ? 47   ILE C CD1   1 
ATOM   5737  N  N     . ALA K  3 48  ? 74.810  24.761  150.096 1.00 18.96 ? 48   ALA C N     1 
ATOM   5738  C  CA    . ALA K  3 48  ? 75.029  23.453  149.507 1.00 18.51 ? 48   ALA C CA    1 
ATOM   5739  C  C     . ALA K  3 48  ? 74.834  22.379  150.580 1.00 21.84 ? 48   ALA C C     1 
ATOM   5740  O  O     . ALA K  3 48  ? 74.257  21.313  150.307 1.00 22.91 ? 48   ALA C O     1 
ATOM   5741  C  CB    . ALA K  3 48  ? 76.441  23.383  148.918 1.00 21.42 ? 48   ALA C CB    1 
ATOM   5742  N  N     . ASP K  3 49  ? 75.291  22.676  151.796 1.00 20.96 ? 49   ASP C N     1 
ATOM   5743  C  CA    . ASP K  3 49  ? 75.153  21.710  152.887 1.00 24.68 ? 49   ASP C CA    1 
ATOM   5744  C  C     . ASP K  3 49  ? 73.679  21.536  153.215 1.00 25.69 ? 49   ASP C C     1 
ATOM   5745  O  O     . ASP K  3 49  ? 73.223  20.410  153.424 1.00 26.99 ? 49   ASP C O     1 
ATOM   5746  C  CB    . ASP K  3 49  ? 75.910  22.154  154.135 1.00 26.03 ? 49   ASP C CB    1 
ATOM   5747  C  CG    . ASP K  3 49  ? 77.410  21.870  154.052 1.00 27.65 ? 49   ASP C CG    1 
ATOM   5748  O  OD1   . ASP K  3 49  ? 77.839  21.069  153.196 1.00 30.61 ? 49   ASP C OD1   1 
ATOM   5749  O  OD2   . ASP K  3 49  ? 78.144  22.455  154.858 1.00 32.79 ? 49   ASP C OD2   1 
ATOM   5750  N  N     . LEU K  3 50  ? 72.924  22.633  153.244 1.00 23.90 ? 50   LEU C N     1 
ATOM   5751  C  CA    . LEU K  3 50  ? 71.502  22.505  153.526 1.00 25.09 ? 50   LEU C CA    1 
ATOM   5752  C  C     . LEU K  3 50  ? 70.741  21.825  152.393 1.00 26.81 ? 50   LEU C C     1 
ATOM   5753  O  O     . LEU K  3 50  ? 69.635  21.327  152.611 1.00 29.30 ? 50   LEU C O     1 
ATOM   5754  C  CB    . LEU K  3 50  ? 70.898  23.866  153.869 1.00 24.54 ? 50   LEU C CB    1 
ATOM   5755  C  CG    . LEU K  3 50  ? 71.459  24.505  155.145 1.00 24.37 ? 50   LEU C CG    1 
ATOM   5756  C  CD1   . LEU K  3 50  ? 70.973  25.911  155.290 1.00 24.93 ? 50   LEU C CD1   1 
ATOM   5757  C  CD2   . LEU K  3 50  ? 71.066  23.658  156.385 1.00 29.40 ? 50   LEU C CD2   1 
ATOM   5758  N  N     . LEU K  3 51  ? 71.304  21.791  151.182 1.00 23.33 ? 51   LEU C N     1 
ATOM   5759  C  CA    . LEU K  3 51  ? 70.642  21.091  150.079 1.00 26.40 ? 51   LEU C CA    1 
ATOM   5760  C  C     . LEU K  3 51  ? 71.130  19.634  150.020 1.00 29.09 ? 51   LEU C C     1 
ATOM   5761  O  O     . LEU K  3 51  ? 70.770  18.887  149.109 1.00 29.41 ? 51   LEU C O     1 
ATOM   5762  C  CB    . LEU K  3 51  ? 70.927  21.791  148.738 1.00 26.32 ? 51   LEU C CB    1 
ATOM   5763  C  CG    . LEU K  3 51  ? 70.453  23.251  148.653 1.00 28.78 ? 51   LEU C CG    1 
ATOM   5764  C  CD1   . LEU K  3 51  ? 70.719  23.771  147.235 1.00 32.32 ? 51   LEU C CD1   1 
ATOM   5765  C  CD2   . LEU K  3 51  ? 68.961  23.371  148.979 1.00 30.60 ? 51   LEU C CD2   1 
ATOM   5766  N  N     . HIS K  3 52  ? 71.968  19.256  150.988 1.00 31.66 ? 52   HIS C N     1 
ATOM   5767  C  CA    . HIS K  3 52  ? 72.543  17.906  151.091 1.00 33.67 ? 52   HIS C CA    1 
ATOM   5768  C  C     . HIS K  3 52  ? 73.415  17.562  149.891 1.00 34.67 ? 52   HIS C C     1 
ATOM   5769  O  O     . HIS K  3 52  ? 73.408  16.432  149.388 1.00 35.10 ? 52   HIS C O     1 
ATOM   5770  C  CB    . HIS K  3 52  ? 71.421  16.869  151.256 1.00 40.25 ? 52   HIS C CB    1 
ATOM   5771  C  CG    . HIS K  3 52  ? 70.492  17.178  152.391 1.00 45.99 ? 52   HIS C CG    1 
ATOM   5772  N  ND1   . HIS K  3 52  ? 70.920  17.253  153.700 1.00 46.76 ? 52   HIS C ND1   1 
ATOM   5773  C  CD2   . HIS K  3 52  ? 69.171  17.477  152.411 1.00 48.97 ? 52   HIS C CD2   1 
ATOM   5774  C  CE1   . HIS K  3 52  ? 69.904  17.586  154.476 1.00 47.22 ? 52   HIS C CE1   1 
ATOM   5775  N  NE2   . HIS K  3 52  ? 68.830  17.728  153.718 1.00 51.52 ? 52   HIS C NE2   1 
ATOM   5776  N  N     . SER K  3 53  ? 74.169  18.548  149.424 1.00 29.89 ? 53   SER C N     1 
ATOM   5777  C  CA    . SER K  3 53  ? 75.042  18.329  148.288 1.00 29.04 ? 53   SER C CA    1 
ATOM   5778  C  C     . SER K  3 53  ? 76.275  17.557  148.733 1.00 30.07 ? 53   SER C C     1 
ATOM   5779  O  O     . SER K  3 53  ? 76.895  17.899  149.737 1.00 30.32 ? 53   SER C O     1 
ATOM   5780  C  CB    . SER K  3 53  ? 75.480  19.661  147.697 1.00 27.45 ? 53   SER C CB    1 
ATOM   5781  O  OG    . SER K  3 53  ? 76.438  19.463  146.670 1.00 25.78 ? 53   SER C OG    1 
ATOM   5782  N  N     . GLU K  3 54  ? 76.622  16.525  147.978 1.00 30.68 ? 54   GLU C N     1 
ATOM   5783  C  CA    . GLU K  3 54  ? 77.793  15.726  148.278 1.00 35.27 ? 54   GLU C CA    1 
ATOM   5784  C  C     . GLU K  3 54  ? 78.682  15.551  147.045 1.00 35.18 ? 54   GLU C C     1 
ATOM   5785  O  O     . GLU K  3 54  ? 79.788  15.018  147.154 1.00 37.48 ? 54   GLU C O     1 
ATOM   5786  C  CB    . GLU K  3 54  ? 77.371  14.352  148.819 1.00 42.43 ? 54   GLU C CB    1 
ATOM   5787  C  CG    . GLU K  3 54  ? 76.632  14.422  150.159 1.00 51.34 ? 54   GLU C CG    1 
ATOM   5788  C  CD    . GLU K  3 54  ? 76.123  13.068  150.647 1.00 57.29 ? 54   GLU C CD    1 
ATOM   5789  O  OE1   . GLU K  3 54  ? 76.516  12.029  150.068 1.00 60.04 ? 54   GLU C OE1   1 
ATOM   5790  O  OE2   . GLU K  3 54  ? 75.334  13.042  151.621 1.00 60.04 ? 54   GLU C OE2   1 
ATOM   5791  N  N     . THR K  3 55  ? 78.241  16.012  145.875 1.00 33.05 ? 55   THR C N     1 
ATOM   5792  C  CA    . THR K  3 55  ? 79.086  15.821  144.698 1.00 32.39 ? 55   THR C CA    1 
ATOM   5793  C  C     . THR K  3 55  ? 80.254  16.793  144.583 1.00 26.96 ? 55   THR C C     1 
ATOM   5794  O  O     . THR K  3 55  ? 80.144  17.994  144.858 1.00 25.08 ? 55   THR C O     1 
ATOM   5795  C  CB    . THR K  3 55  ? 78.295  15.863  143.371 1.00 37.99 ? 55   THR C CB    1 
ATOM   5796  O  OG1   . THR K  3 55  ? 77.403  14.739  143.297 1.00 43.00 ? 55   THR C OG1   1 
ATOM   5797  C  CG2   . THR K  3 55  ? 79.262  15.788  142.182 1.00 39.60 ? 55   THR C CG2   1 
ATOM   5798  N  N     . VAL K  3 56  ? 81.382  16.226  144.193 1.00 27.57 ? 56   VAL C N     1 
ATOM   5799  C  CA    . VAL K  3 56  ? 82.604  16.969  144.003 1.00 26.17 ? 56   VAL C CA    1 
ATOM   5800  C  C     . VAL K  3 56  ? 82.852  16.901  142.520 1.00 29.54 ? 56   VAL C C     1 
ATOM   5801  O  O     . VAL K  3 56  ? 82.798  15.830  141.918 1.00 33.97 ? 56   VAL C O     1 
ATOM   5802  C  CB    . VAL K  3 56  ? 83.765  16.331  144.784 1.00 30.17 ? 56   VAL C CB    1 
ATOM   5803  C  CG1   . VAL K  3 56  ? 85.080  17.025  144.442 1.00 34.19 ? 56   VAL C CG1   1 
ATOM   5804  C  CG2   . VAL K  3 56  ? 83.481  16.441  146.275 1.00 29.20 ? 56   VAL C CG2   1 
ATOM   5805  N  N     . SER K  3 57  ? 83.115  18.053  141.926 1.00 26.32 ? 57   SER C N     1 
ATOM   5806  C  CA    . SER K  3 57  ? 83.342  18.128  140.504 1.00 25.83 ? 57   SER C CA    1 
ATOM   5807  C  C     . SER K  3 57  ? 84.012  19.462  140.234 1.00 22.42 ? 57   SER C C     1 
ATOM   5808  O  O     . SER K  3 57  ? 83.824  20.427  140.987 1.00 21.81 ? 57   SER C O     1 
ATOM   5809  C  CB    . SER K  3 57  ? 81.996  18.082  139.767 1.00 27.99 ? 57   SER C CB    1 
ATOM   5810  O  OG    . SER K  3 57  ? 82.172  18.429  138.405 1.00 37.07 ? 57   SER C OG    1 
ATOM   5811  N  N     . GLU K  3 58  ? 84.816  19.528  139.188 1.00 25.16 ? 58   GLU C N     1 
ATOM   5812  C  CA    . GLU K  3 58  ? 85.408  20.811  138.891 1.00 27.15 ? 58   GLU C CA    1 
ATOM   5813  C  C     . GLU K  3 58  ? 84.265  21.639  138.305 1.00 26.70 ? 58   GLU C C     1 
ATOM   5814  O  O     . GLU K  3 58  ? 83.274  21.116  137.777 1.00 22.70 ? 58   GLU C O     1 
ATOM   5815  C  CB    . GLU K  3 58  ? 86.604  20.649  137.953 1.00 33.78 ? 58   GLU C CB    1 
ATOM   5816  C  CG    . GLU K  3 58  ? 87.792  19.976  138.686 1.00 36.29 ? 58   GLU C CG    1 
ATOM   5817  C  CD    . GLU K  3 58  ? 88.188  20.697  139.998 1.00 39.76 ? 58   GLU C CD    1 
ATOM   5818  O  OE1   . GLU K  3 58  ? 88.808  21.785  139.920 1.00 39.81 ? 58   GLU C OE1   1 
ATOM   5819  O  OE2   . GLU K  3 58  ? 87.873  20.189  141.109 1.00 29.04 ? 58   GLU C OE2   1 
ATOM   5820  N  N     . ARG K  3 59  ? 84.381  22.941  138.472 1.00 25.84 ? 59   ARG C N     1 
ATOM   5821  C  CA    . ARG K  3 59  ? 83.362  23.872  138.031 1.00 23.34 ? 59   ARG C CA    1 
ATOM   5822  C  C     . ARG K  3 59  ? 83.081  23.740  136.542 1.00 21.69 ? 59   ARG C C     1 
ATOM   5823  O  O     . ARG K  3 59  ? 84.003  23.689  135.749 1.00 21.94 ? 59   ARG C O     1 
ATOM   5824  C  CB    . ARG K  3 59  ? 83.867  25.264  138.322 1.00 24.80 ? 59   ARG C CB    1 
ATOM   5825  C  CG    . ARG K  3 59  ? 82.827  26.335  138.326 1.00 25.42 ? 59   ARG C CG    1 
ATOM   5826  C  CD    . ARG K  3 59  ? 83.535  27.600  138.749 1.00 25.23 ? 59   ARG C CD    1 
ATOM   5827  N  NE    . ARG K  3 59  ? 82.570  28.597  139.121 1.00 30.70 ? 59   ARG C NE    1 
ATOM   5828  C  CZ    . ARG K  3 59  ? 82.482  29.172  140.309 1.00 25.01 ? 59   ARG C CZ    1 
ATOM   5829  N  NH1   . ARG K  3 59  ? 83.316  28.867  141.311 1.00 27.08 ? 59   ARG C NH1   1 
ATOM   5830  N  NH2   . ARG K  3 59  ? 81.545  30.075  140.481 1.00 26.41 ? 59   ARG C NH2   1 
ATOM   5831  N  N     . LEU K  3 60  ? 81.805  23.712  136.174 1.00 23.20 ? 60   LEU C N     1 
ATOM   5832  C  CA    . LEU K  3 60  ? 81.467  23.608  134.773 1.00 21.55 ? 60   LEU C CA    1 
ATOM   5833  C  C     . LEU K  3 60  ? 81.737  24.937  134.075 1.00 20.07 ? 60   LEU C C     1 
ATOM   5834  O  O     . LEU K  3 60  ? 81.777  26.005  134.708 1.00 20.60 ? 60   LEU C O     1 
ATOM   5835  C  CB    . LEU K  3 60  ? 79.988  23.262  134.604 1.00 21.80 ? 60   LEU C CB    1 
ATOM   5836  C  CG    . LEU K  3 60  ? 79.474  21.954  135.202 1.00 27.08 ? 60   LEU C CG    1 
ATOM   5837  C  CD1   . LEU K  3 60  ? 77.996  21.789  134.851 1.00 25.28 ? 60   LEU C CD1   1 
ATOM   5838  C  CD2   . LEU K  3 60  ? 80.282  20.778  134.638 1.00 27.76 ? 60   LEU C CD2   1 
ATOM   5839  N  N     . PRO K  3 61  ? 81.967  24.883  132.758 1.00 20.27 ? 61   PRO C N     1 
ATOM   5840  C  CA    . PRO K  3 61  ? 82.204  26.126  132.012 1.00 16.59 ? 61   PRO C CA    1 
ATOM   5841  C  C     . PRO K  3 61  ? 80.955  26.993  132.238 1.00 16.37 ? 61   PRO C C     1 
ATOM   5842  O  O     . PRO K  3 61  ? 79.837  26.467  132.312 1.00 16.84 ? 61   PRO C O     1 
ATOM   5843  C  CB    . PRO K  3 61  ? 82.281  25.649  130.571 1.00 19.14 ? 61   PRO C CB    1 
ATOM   5844  C  CG    . PRO K  3 61  ? 82.896  24.263  130.699 1.00 19.76 ? 61   PRO C CG    1 
ATOM   5845  C  CD    . PRO K  3 61  ? 82.145  23.691  131.907 1.00 20.49 ? 61   PRO C CD    1 
ATOM   5846  N  N     . GLY K  3 62  ? 81.136  28.310  132.310 1.00 18.56 ? 62   GLY C N     1 
ATOM   5847  C  CA    . GLY K  3 62  ? 79.998  29.197  132.542 1.00 16.16 ? 62   GLY C CA    1 
ATOM   5848  C  C     . GLY K  3 62  ? 78.902  29.069  131.502 1.00 17.47 ? 62   GLY C C     1 
ATOM   5849  O  O     . GLY K  3 62  ? 77.718  29.236  131.799 1.00 16.13 ? 62   GLY C O     1 
ATOM   5850  N  N     . GLN K  3 63  ? 79.285  28.784  130.261 1.00 18.19 ? 63   GLN C N     1 
ATOM   5851  C  CA    . GLN K  3 63  ? 78.278  28.638  129.217 1.00 17.81 ? 63   GLN C CA    1 
ATOM   5852  C  C     . GLN K  3 63  ? 77.399  27.424  129.492 1.00 15.28 ? 63   GLN C C     1 
ATOM   5853  O  O     . GLN K  3 63  ? 76.196  27.412  129.180 1.00 15.64 ? 63   GLN C O     1 
ATOM   5854  C  CB    . GLN K  3 63  ? 78.955  28.472  127.850 1.00 18.97 ? 63   GLN C CB    1 
ATOM   5855  C  CG    . GLN K  3 63  ? 79.923  29.605  127.520 1.00 16.06 ? 63   GLN C CG    1 
ATOM   5856  C  CD    . GLN K  3 63  ? 81.348  29.334  127.975 1.00 18.35 ? 63   GLN C CD    1 
ATOM   5857  O  OE1   . GLN K  3 63  ? 81.584  28.570  128.914 1.00 19.09 ? 63   GLN C OE1   1 
ATOM   5858  N  NE2   . GLN K  3 63  ? 82.306  29.985  127.324 1.00 18.29 ? 63   GLN C NE2   1 
ATOM   5859  N  N     . THR K  3 64  ? 78.007  26.390  130.068 1.00 13.69 ? 64   THR C N     1 
ATOM   5860  C  CA    . THR K  3 64  ? 77.286  25.172  130.364 1.00 16.43 ? 64   THR C CA    1 
ATOM   5861  C  C     . THR K  3 64  ? 76.331  25.379  131.534 1.00 15.27 ? 64   THR C C     1 
ATOM   5862  O  O     . THR K  3 64  ? 75.150  25.019  131.445 1.00 16.43 ? 64   THR C O     1 
ATOM   5863  C  CB    . THR K  3 64  ? 78.281  24.022  130.663 1.00 18.27 ? 64   THR C CB    1 
ATOM   5864  O  OG1   . THR K  3 64  ? 79.099  23.827  129.503 1.00 21.51 ? 64   THR C OG1   1 
ATOM   5865  C  CG2   . THR K  3 64  ? 77.536  22.712  130.992 1.00 16.98 ? 64   THR C CG2   1 
ATOM   5866  N  N     . SER K  3 65  ? 76.827  25.942  132.625 1.00 16.81 ? 65   SER C N     1 
ATOM   5867  C  CA    . SER K  3 65  ? 75.945  26.169  133.766 1.00 17.29 ? 65   SER C CA    1 
ATOM   5868  C  C     . SER K  3 65  ? 74.848  27.182  133.443 1.00 15.34 ? 65   SER C C     1 
ATOM   5869  O  O     . SER K  3 65  ? 73.704  27.030  133.899 1.00 15.77 ? 65   SER C O     1 
ATOM   5870  C  CB    . SER K  3 65  ? 76.737  26.637  134.978 1.00 15.81 ? 65   SER C CB    1 
ATOM   5871  O  OG    . SER K  3 65  ? 77.502  27.791  134.682 1.00 20.24 ? 65   SER C OG    1 
ATOM   5872  N  N     . GLY K  3 66  ? 75.185  28.212  132.664 1.00 16.21 ? 66   GLY C N     1 
ATOM   5873  C  CA    . GLY K  3 66  ? 74.178  29.199  132.283 1.00 15.06 ? 66   GLY C CA    1 
ATOM   5874  C  C     . GLY K  3 66  ? 73.022  28.537  131.537 1.00 15.77 ? 66   GLY C C     1 
ATOM   5875  O  O     . GLY K  3 66  ? 71.840  28.742  131.833 1.00 16.46 ? 66   GLY C O     1 
ATOM   5876  N  N     . ASN K  3 67  ? 73.356  27.719  130.551 1.00 14.50 ? 67   ASN C N     1 
ATOM   5877  C  CA    . ASN K  3 67  ? 72.338  27.036  129.773 1.00 16.13 ? 67   ASN C CA    1 
ATOM   5878  C  C     . ASN K  3 67  ? 71.562  26.005  130.600 1.00 16.08 ? 67   ASN C C     1 
ATOM   5879  O  O     . ASN K  3 67  ? 70.332  25.912  130.495 1.00 16.06 ? 67   ASN C O     1 
ATOM   5880  C  CB    . ASN K  3 67  ? 73.007  26.352  128.569 1.00 16.84 ? 67   ASN C CB    1 
ATOM   5881  C  CG    . ASN K  3 67  ? 71.998  25.632  127.675 1.00 22.26 ? 67   ASN C CG    1 
ATOM   5882  O  OD1   . ASN K  3 67  ? 71.113  26.251  127.078 1.00 22.72 ? 67   ASN C OD1   1 
ATOM   5883  N  ND2   . ASN K  3 67  ? 72.122  24.323  127.598 1.00 23.91 ? 67   ASN C ND2   1 
ATOM   5884  N  N     . ALA K  3 68  ? 72.277  25.219  131.402 1.00 15.93 ? 68   ALA C N     1 
ATOM   5885  C  CA    . ALA K  3 68  ? 71.628  24.180  132.220 1.00 16.71 ? 68   ALA C CA    1 
ATOM   5886  C  C     . ALA K  3 68  ? 70.696  24.812  133.266 1.00 17.41 ? 68   ALA C C     1 
ATOM   5887  O  O     . ALA K  3 68  ? 69.585  24.320  133.494 1.00 17.22 ? 68   ALA C O     1 
ATOM   5888  C  CB    . ALA K  3 68  ? 72.705  23.290  132.913 1.00 17.07 ? 68   ALA C CB    1 
ATOM   5889  N  N     . PHE K  3 69  ? 71.136  25.912  133.879 1.00 16.35 ? 69   PHE C N     1 
ATOM   5890  C  CA    . PHE K  3 69  ? 70.293  26.583  134.859 1.00 15.52 ? 69   PHE C CA    1 
ATOM   5891  C  C     . PHE K  3 69  ? 69.006  27.054  134.188 1.00 14.90 ? 69   PHE C C     1 
ATOM   5892  O  O     . PHE K  3 69  ? 67.915  26.915  134.753 1.00 16.33 ? 69   PHE C O     1 
ATOM   5893  C  CB    . PHE K  3 69  ? 71.047  27.749  135.520 1.00 15.95 ? 69   PHE C CB    1 
ATOM   5894  C  CG    . PHE K  3 69  ? 70.294  28.410  136.658 1.00 16.99 ? 69   PHE C CG    1 
ATOM   5895  C  CD1   . PHE K  3 69  ? 69.855  27.670  137.769 1.00 15.39 ? 69   PHE C CD1   1 
ATOM   5896  C  CD2   . PHE K  3 69  ? 70.065  29.779  136.646 1.00 16.03 ? 69   PHE C CD2   1 
ATOM   5897  C  CE1   . PHE K  3 69  ? 69.210  28.301  138.845 1.00 17.73 ? 69   PHE C CE1   1 
ATOM   5898  C  CE2   . PHE K  3 69  ? 69.420  30.427  137.705 1.00 18.15 ? 69   PHE C CE2   1 
ATOM   5899  C  CZ    . PHE K  3 69  ? 68.987  29.680  138.817 1.00 19.09 ? 69   PHE C CZ    1 
ATOM   5900  N  N     . GLU K  3 70  ? 69.113  27.617  132.981 1.00 15.41 ? 70   GLU C N     1 
ATOM   5901  C  CA    . GLU K  3 70  ? 67.912  28.033  132.257 1.00 15.27 ? 70   GLU C CA    1 
ATOM   5902  C  C     . GLU K  3 70  ? 66.972  26.843  132.039 1.00 15.40 ? 70   GLU C C     1 
ATOM   5903  O  O     . GLU K  3 70  ? 65.772  26.934  132.295 1.00 15.67 ? 70   GLU C O     1 
ATOM   5904  C  CB    . GLU K  3 70  ? 68.272  28.605  130.874 1.00 15.19 ? 70   GLU C CB    1 
ATOM   5905  C  CG    . GLU K  3 70  ? 68.845  30.023  130.891 1.00 17.65 ? 70   GLU C CG    1 
ATOM   5906  C  CD    . GLU K  3 70  ? 69.248  30.491  129.499 1.00 20.85 ? 70   GLU C CD    1 
ATOM   5907  O  OE1   . GLU K  3 70  ? 68.922  29.788  128.511 1.00 20.42 ? 70   GLU C OE1   1 
ATOM   5908  O  OE2   . GLU K  3 70  ? 69.902  31.545  129.404 1.00 22.06 ? 70   GLU C OE2   1 
ATOM   5909  N  N     . ALA K  3 71  ? 67.522  25.735  131.533 1.00 15.55 ? 71   ALA C N     1 
ATOM   5910  C  CA    . ALA K  3 71  ? 66.707  24.544  131.266 1.00 16.73 ? 71   ALA C CA    1 
ATOM   5911  C  C     . ALA K  3 71  ? 66.006  24.013  132.514 1.00 16.84 ? 71   ALA C C     1 
ATOM   5912  O  O     . ALA K  3 71  ? 64.819  23.720  132.474 1.00 16.60 ? 71   ALA C O     1 
ATOM   5913  C  CB    . ALA K  3 71  ? 67.580  23.439  130.648 1.00 17.25 ? 71   ALA C CB    1 
ATOM   5914  N  N     . ILE K  3 72  ? 66.736  23.905  133.616 1.00 17.70 ? 72   ILE C N     1 
ATOM   5915  C  CA    . ILE K  3 72  ? 66.151  23.395  134.849 1.00 16.84 ? 72   ILE C CA    1 
ATOM   5916  C  C     . ILE K  3 72  ? 65.102  24.333  135.445 1.00 18.16 ? 72   ILE C C     1 
ATOM   5917  O  O     . ILE K  3 72  ? 64.074  23.867  135.948 1.00 15.83 ? 72   ILE C O     1 
ATOM   5918  C  CB    . ILE K  3 72  ? 67.271  23.025  135.853 1.00 19.27 ? 72   ILE C CB    1 
ATOM   5919  C  CG1   . ILE K  3 72  ? 68.010  21.793  135.294 1.00 19.09 ? 72   ILE C CG1   1 
ATOM   5920  C  CG2   . ILE K  3 72  ? 66.683  22.761  137.257 1.00 16.81 ? 72   ILE C CG2   1 
ATOM   5921  C  CD1   . ILE K  3 72  ? 69.392  21.546  135.882 1.00 18.65 ? 72   ILE C CD1   1 
ATOM   5922  N  N     . CYS K  3 73  ? 65.343  25.644  135.392 1.00 17.33 ? 73   CYS C N     1 
ATOM   5923  C  CA    . CYS K  3 73  ? 64.339  26.593  135.872 1.00 15.86 ? 73   CYS C CA    1 
ATOM   5924  C  C     . CYS K  3 73  ? 63.078  26.454  135.015 1.00 15.83 ? 73   CYS C C     1 
ATOM   5925  O  O     . CYS K  3 73  ? 61.966  26.492  135.513 1.00 14.70 ? 73   CYS C O     1 
ATOM   5926  C  CB    . CYS K  3 73  ? 64.839  28.041  135.771 1.00 15.51 ? 73   CYS C CB    1 
ATOM   5927  S  SG    . CYS K  3 73  ? 66.039  28.500  137.045 1.00 16.81 ? 73   CYS C SG    1 
ATOM   5928  N  N     . SER K  3 74  ? 63.252  26.324  133.709 1.00 15.50 ? 74   SER C N     1 
ATOM   5929  C  CA    . SER K  3 74  ? 62.117  26.197  132.822 1.00 14.30 ? 74   SER C CA    1 
ATOM   5930  C  C     . SER K  3 74  ? 61.255  24.974  133.159 1.00 16.50 ? 74   SER C C     1 
ATOM   5931  O  O     . SER K  3 74  ? 60.031  25.059  133.153 1.00 17.08 ? 74   SER C O     1 
ATOM   5932  C  CB    . SER K  3 74  ? 62.610  26.095  131.378 1.00 17.91 ? 74   SER C CB    1 
ATOM   5933  O  OG    . SER K  3 74  ? 61.507  26.123  130.512 1.00 26.53 ? 74   SER C OG    1 
ATOM   5934  N  N     . GLU K  3 75  ? 61.908  23.847  133.436 1.00 16.89 ? 75   GLU C N     1 
ATOM   5935  C  CA    . GLU K  3 75  ? 61.177  22.617  133.771 1.00 16.45 ? 75   GLU C CA    1 
ATOM   5936  C  C     . GLU K  3 75  ? 60.414  22.777  135.093 1.00 17.37 ? 75   GLU C C     1 
ATOM   5937  O  O     . GLU K  3 75  ? 59.281  22.297  135.205 1.00 19.51 ? 75   GLU C O     1 
ATOM   5938  C  CB    . GLU K  3 75  ? 62.149  21.428  133.838 1.00 18.56 ? 75   GLU C CB    1 
ATOM   5939  C  CG    . GLU K  3 75  ? 62.722  21.089  132.469 1.00 24.89 ? 75   GLU C CG    1 
ATOM   5940  C  CD    . GLU K  3 75  ? 63.778  20.007  132.522 1.00 33.38 ? 75   GLU C CD    1 
ATOM   5941  O  OE1   . GLU K  3 75  ? 64.147  19.579  133.638 1.00 32.49 ? 75   GLU C OE1   1 
ATOM   5942  O  OE2   . GLU K  3 75  ? 64.244  19.587  131.441 1.00 35.90 ? 75   GLU C OE2   1 
ATOM   5943  N  N     . PHE K  3 76  ? 61.024  23.441  136.078 1.00 17.21 ? 76   PHE C N     1 
ATOM   5944  C  CA    . PHE K  3 76  ? 60.358  23.664  137.373 1.00 18.00 ? 76   PHE C CA    1 
ATOM   5945  C  C     . PHE K  3 76  ? 59.119  24.522  137.150 1.00 18.17 ? 76   PHE C C     1 
ATOM   5946  O  O     . PHE K  3 76  ? 58.025  24.192  137.609 1.00 16.70 ? 76   PHE C O     1 
ATOM   5947  C  CB    . PHE K  3 76  ? 61.287  24.379  138.361 1.00 17.77 ? 76   PHE C CB    1 
ATOM   5948  C  CG    . PHE K  3 76  ? 60.583  24.896  139.589 1.00 19.16 ? 76   PHE C CG    1 
ATOM   5949  C  CD1   . PHE K  3 76  ? 60.230  24.034  140.624 1.00 21.90 ? 76   PHE C CD1   1 
ATOM   5950  C  CD2   . PHE K  3 76  ? 60.226  26.249  139.690 1.00 21.50 ? 76   PHE C CD2   1 
ATOM   5951  C  CE1   . PHE K  3 76  ? 59.531  24.510  141.741 1.00 19.50 ? 76   PHE C CE1   1 
ATOM   5952  C  CE2   . PHE K  3 76  ? 59.529  26.730  140.792 1.00 22.29 ? 76   PHE C CE2   1 
ATOM   5953  C  CZ    . PHE K  3 76  ? 59.179  25.864  141.823 1.00 23.17 ? 76   PHE C CZ    1 
ATOM   5954  N  N     . VAL K  3 77  ? 59.283  25.636  136.440 1.00 17.15 ? 77   VAL C N     1 
ATOM   5955  C  CA    . VAL K  3 77  ? 58.147  26.505  136.186 1.00 16.75 ? 77   VAL C CA    1 
ATOM   5956  C  C     . VAL K  3 77  ? 57.009  25.783  135.444 1.00 17.62 ? 77   VAL C C     1 
ATOM   5957  O  O     . VAL K  3 77  ? 55.844  25.942  135.798 1.00 19.10 ? 77   VAL C O     1 
ATOM   5958  C  CB    . VAL K  3 77  ? 58.577  27.758  135.381 1.00 16.39 ? 77   VAL C CB    1 
ATOM   5959  C  CG1   . VAL K  3 77  ? 57.357  28.562  134.948 1.00 18.21 ? 77   VAL C CG1   1 
ATOM   5960  C  CG2   . VAL K  3 77  ? 59.492  28.606  136.228 1.00 19.75 ? 77   VAL C CG2   1 
ATOM   5961  N  N     . GLN K  3 78  ? 57.340  25.013  134.406 1.00 17.13 ? 78   GLN C N     1 
ATOM   5962  C  CA    . GLN K  3 78  ? 56.329  24.300  133.642 1.00 17.27 ? 78   GLN C CA    1 
ATOM   5963  C  C     . GLN K  3 78  ? 55.563  23.327  134.536 1.00 17.88 ? 78   GLN C C     1 
ATOM   5964  O  O     . GLN K  3 78  ? 54.322  23.347  134.580 1.00 18.90 ? 78   GLN C O     1 
ATOM   5965  C  CB    . GLN K  3 78  ? 56.995  23.546  132.483 1.00 21.43 ? 78   GLN C CB    1 
ATOM   5966  C  CG    . GLN K  3 78  ? 56.026  22.831  131.540 1.00 25.60 ? 78   GLN C CG    1 
ATOM   5967  C  CD    . GLN K  3 78  ? 55.366  21.625  132.195 1.00 35.82 ? 78   GLN C CD    1 
ATOM   5968  O  OE1   . GLN K  3 78  ? 56.026  20.844  132.892 1.00 38.38 ? 78   GLN C OE1   1 
ATOM   5969  N  NE2   . GLN K  3 78  ? 54.059  21.464  131.970 1.00 38.10 ? 78   GLN C NE2   1 
ATOM   5970  N  N     . SER K  3 79  ? 56.297  22.517  135.289 1.00 18.24 ? 79   SER C N     1 
ATOM   5971  C  CA    . SER K  3 79  ? 55.652  21.534  136.153 1.00 18.80 ? 79   SER C CA    1 
ATOM   5972  C  C     . SER K  3 79  ? 54.753  22.119  137.234 1.00 18.86 ? 79   SER C C     1 
ATOM   5973  O  O     . SER K  3 79  ? 53.604  21.675  137.419 1.00 20.46 ? 79   SER C O     1 
ATOM   5974  C  CB    . SER K  3 79  ? 56.705  20.634  136.800 1.00 23.21 ? 79   SER C CB    1 
ATOM   5975  O  OG    . SER K  3 79  ? 56.042  19.591  137.500 1.00 26.59 ? 79   SER C OG    1 
ATOM   5976  N  N     . ALA K  3 80  ? 55.255  23.118  137.947 1.00 18.48 ? 80   ALA C N     1 
ATOM   5977  C  CA    . ALA K  3 80  ? 54.477  23.714  139.012 1.00 19.09 ? 80   ALA C CA    1 
ATOM   5978  C  C     . ALA K  3 80  ? 53.320  24.574  138.509 1.00 20.03 ? 80   ALA C C     1 
ATOM   5979  O  O     . ALA K  3 80  ? 52.231  24.539  139.074 1.00 18.72 ? 80   ALA C O     1 
ATOM   5980  C  CB    . ALA K  3 80  ? 55.384  24.527  139.936 1.00 19.03 ? 80   ALA C CB    1 
ATOM   5981  N  N     . PHE K  3 81  ? 53.544  25.363  137.452 1.00 18.07 ? 81   PHE C N     1 
ATOM   5982  C  CA    . PHE K  3 81  ? 52.475  26.224  136.956 1.00 17.54 ? 81   PHE C CA    1 
ATOM   5983  C  C     . PHE K  3 81  ? 51.316  25.388  136.405 1.00 17.56 ? 81   PHE C C     1 
ATOM   5984  O  O     . PHE K  3 81  ? 50.150  25.797  136.486 1.00 18.89 ? 81   PHE C O     1 
ATOM   5985  C  CB    . PHE K  3 81  ? 53.026  27.180  135.867 1.00 17.46 ? 81   PHE C CB    1 
ATOM   5986  C  CG    . PHE K  3 81  ? 52.064  28.257  135.461 1.00 15.21 ? 81   PHE C CG    1 
ATOM   5987  C  CD1   . PHE K  3 81  ? 51.593  29.178  136.388 1.00 17.15 ? 81   PHE C CD1   1 
ATOM   5988  C  CD2   . PHE K  3 81  ? 51.645  28.366  134.141 1.00 19.36 ? 81   PHE C CD2   1 
ATOM   5989  C  CE1   . PHE K  3 81  ? 50.717  30.189  136.018 1.00 17.25 ? 81   PHE C CE1   1 
ATOM   5990  C  CE2   . PHE K  3 81  ? 50.761  29.377  133.749 1.00 16.89 ? 81   PHE C CE2   1 
ATOM   5991  C  CZ    . PHE K  3 81  ? 50.297  30.289  134.688 1.00 17.89 ? 81   PHE C CZ    1 
ATOM   5992  N  N     . GLU K  3 82  ? 51.647  24.224  135.843 1.00 16.95 ? 82   GLU C N     1 
ATOM   5993  C  CA    . GLU K  3 82  ? 50.643  23.323  135.284 1.00 20.87 ? 82   GLU C CA    1 
ATOM   5994  C  C     . GLU K  3 82  ? 49.578  22.965  136.322 1.00 19.00 ? 82   GLU C C     1 
ATOM   5995  O  O     . GLU K  3 82  ? 48.425  22.728  135.974 1.00 21.18 ? 82   GLU C O     1 
ATOM   5996  C  CB    . GLU K  3 82  ? 51.349  22.063  134.763 1.00 24.51 ? 82   GLU C CB    1 
ATOM   5997  C  CG    . GLU K  3 82  ? 50.541  21.111  133.912 1.00 36.36 ? 82   GLU C CG    1 
ATOM   5998  C  CD    . GLU K  3 82  ? 51.439  20.017  133.326 1.00 45.07 ? 82   GLU C CD    1 
ATOM   5999  O  OE1   . GLU K  3 82  ? 52.176  19.370  134.111 1.00 49.62 ? 82   GLU C OE1   1 
ATOM   6000  O  OE2   . GLU K  3 82  ? 51.420  19.800  132.089 1.00 50.10 ? 82   GLU C OE2   1 
ATOM   6001  N  N     . LYS K  3 83  ? 49.952  22.959  137.594 1.00 18.84 ? 83   LYS C N     1 
ATOM   6002  C  CA    . LYS K  3 83  ? 49.021  22.621  138.670 1.00 20.11 ? 83   LYS C CA    1 
ATOM   6003  C  C     . LYS K  3 83  ? 48.090  23.757  139.104 1.00 20.31 ? 83   LYS C C     1 
ATOM   6004  O  O     . LYS K  3 83  ? 47.236  23.576  139.975 1.00 20.92 ? 83   LYS C O     1 
ATOM   6005  C  CB    . LYS K  3 83  ? 49.827  22.117  139.865 1.00 20.78 ? 83   LYS C CB    1 
ATOM   6006  C  CG    . LYS K  3 83  ? 50.530  20.797  139.525 1.00 28.32 ? 83   LYS C CG    1 
ATOM   6007  C  CD    . LYS K  3 83  ? 51.340  20.201  140.654 1.00 33.65 ? 83   LYS C CD    1 
ATOM   6008  C  CE    . LYS K  3 83  ? 51.796  18.771  140.289 1.00 34.37 ? 83   LYS C CE    1 
ATOM   6009  N  NZ    . LYS K  3 83  ? 52.551  18.674  139.001 1.00 40.00 ? 83   LYS C NZ    1 
ATOM   6010  N  N     . LEU K  3 84  ? 48.223  24.926  138.476 1.00 19.39 ? 84   LEU C N     1 
ATOM   6011  C  CA    . LEU K  3 84  ? 47.405  26.077  138.858 1.00 19.44 ? 84   LEU C CA    1 
ATOM   6012  C  C     . LEU K  3 84  ? 46.335  26.434  137.824 1.00 17.89 ? 84   LEU C C     1 
ATOM   6013  O  O     . LEU K  3 84  ? 45.818  27.544  137.825 1.00 19.95 ? 84   LEU C O     1 
ATOM   6014  C  CB    . LEU K  3 84  ? 48.314  27.290  139.103 1.00 18.79 ? 84   LEU C CB    1 
ATOM   6015  C  CG    . LEU K  3 84  ? 49.350  27.051  140.198 1.00 19.85 ? 84   LEU C CG    1 
ATOM   6016  C  CD1   . LEU K  3 84  ? 50.274  28.294  140.333 1.00 21.13 ? 84   LEU C CD1   1 
ATOM   6017  C  CD2   . LEU K  3 84  ? 48.624  26.752  141.515 1.00 19.34 ? 84   LEU C CD2   1 
ATOM   6018  N  N     . GLN K  3 85  ? 46.012  25.474  136.966 1.00 20.98 ? 85   GLN C N     1 
ATOM   6019  C  CA    . GLN K  3 85  ? 45.016  25.672  135.924 1.00 24.40 ? 85   GLN C CA    1 
ATOM   6020  C  C     . GLN K  3 85  ? 43.663  26.155  136.483 1.00 24.83 ? 85   GLN C C     1 
ATOM   6021  O  O     . GLN K  3 85  ? 42.932  26.889  135.808 1.00 24.08 ? 85   GLN C O     1 
ATOM   6022  C  CB    . GLN K  3 85  ? 44.865  24.360  135.133 1.00 26.44 ? 85   GLN C CB    1 
ATOM   6023  C  CG    . GLN K  3 85  ? 43.778  24.357  134.074 1.00 31.25 ? 85   GLN C CG    1 
ATOM   6024  C  CD    . GLN K  3 85  ? 44.163  25.123  132.818 1.00 33.20 ? 85   GLN C CD    1 
ATOM   6025  O  OE1   . GLN K  3 85  ? 43.297  25.506  132.021 1.00 33.73 ? 85   GLN C OE1   1 
ATOM   6026  N  NE2   . GLN K  3 85  ? 45.460  25.334  132.628 1.00 35.49 ? 85   GLN C NE2   1 
ATOM   6027  N  N     . HIS K  3 86  ? 43.318  25.759  137.711 1.00 22.52 ? 86   HIS C N     1 
ATOM   6028  C  CA    . HIS K  3 86  ? 42.047  26.187  138.297 1.00 23.50 ? 86   HIS C CA    1 
ATOM   6029  C  C     . HIS K  3 86  ? 42.021  27.647  138.753 1.00 22.39 ? 86   HIS C C     1 
ATOM   6030  O  O     . HIS K  3 86  ? 40.940  28.214  138.905 1.00 22.79 ? 86   HIS C O     1 
ATOM   6031  C  CB    . HIS K  3 86  ? 41.641  25.264  139.457 1.00 23.40 ? 86   HIS C CB    1 
ATOM   6032  C  CG    . HIS K  3 86  ? 42.591  25.296  140.613 1.00 22.19 ? 86   HIS C CG    1 
ATOM   6033  N  ND1   . HIS K  3 86  ? 43.883  24.824  140.528 1.00 22.34 ? 86   HIS C ND1   1 
ATOM   6034  C  CD2   . HIS K  3 86  ? 42.431  25.731  141.887 1.00 21.85 ? 86   HIS C CD2   1 
ATOM   6035  C  CE1   . HIS K  3 86  ? 44.479  24.963  141.696 1.00 23.90 ? 86   HIS C CE1   1 
ATOM   6036  N  NE2   . HIS K  3 86  ? 43.620  25.509  142.539 1.00 21.54 ? 86   HIS C NE2   1 
ATOM   6037  N  N     . ILE K  3 87  ? 43.186  28.261  139.004 1.00 20.37 ? 87   ILE C N     1 
ATOM   6038  C  CA    . ILE K  3 87  ? 43.198  29.677  139.379 1.00 22.63 ? 87   ILE C CA    1 
ATOM   6039  C  C     . ILE K  3 87  ? 43.698  30.567  138.229 1.00 19.21 ? 87   ILE C C     1 
ATOM   6040  O  O     . ILE K  3 87  ? 43.544  31.794  138.280 1.00 19.52 ? 87   ILE C O     1 
ATOM   6041  C  CB    . ILE K  3 87  ? 44.049  29.983  140.648 1.00 24.23 ? 87   ILE C CB    1 
ATOM   6042  C  CG1   . ILE K  3 87  ? 45.510  29.592  140.435 1.00 26.56 ? 87   ILE C CG1   1 
ATOM   6043  C  CG2   . ILE K  3 87  ? 43.436  29.281  141.886 1.00 25.41 ? 87   ILE C CG2   1 
ATOM   6044  C  CD1   . ILE K  3 87  ? 46.403  30.061  141.584 1.00 26.57 ? 87   ILE C CD1   1 
ATOM   6045  N  N     . ARG K  3 88  ? 44.267  29.947  137.192 1.00 20.75 ? 88   ARG C N     1 
ATOM   6046  C  CA    . ARG K  3 88  ? 44.766  30.707  136.023 1.00 20.12 ? 88   ARG C CA    1 
ATOM   6047  C  C     . ARG K  3 88  ? 44.700  29.756  134.822 1.00 20.18 ? 88   ARG C C     1 
ATOM   6048  O  O     . ARG K  3 88  ? 45.700  29.246  134.342 1.00 19.40 ? 88   ARG C O     1 
ATOM   6049  C  CB    . ARG K  3 88  ? 46.199  31.192  136.269 1.00 19.16 ? 88   ARG C CB    1 
ATOM   6050  C  CG    . ARG K  3 88  ? 46.660  32.331  135.339 1.00 17.10 ? 88   ARG C CG    1 
ATOM   6051  C  CD    . ARG K  3 88  ? 45.854  33.640  135.583 1.00 17.56 ? 88   ARG C CD    1 
ATOM   6052  N  NE    . ARG K  3 88  ? 46.542  34.806  135.030 1.00 18.01 ? 88   ARG C NE    1 
ATOM   6053  C  CZ    . ARG K  3 88  ? 46.444  35.248  133.780 1.00 19.84 ? 88   ARG C CZ    1 
ATOM   6054  N  NH1   . ARG K  3 88  ? 45.663  34.628  132.906 1.00 18.33 ? 88   ARG C NH1   1 
ATOM   6055  N  NH2   . ARG K  3 88  ? 47.146  36.307  133.395 1.00 18.78 ? 88   ARG C NH2   1 
ATOM   6056  N  N     . PRO K  3 89  ? 43.486  29.489  134.343 1.00 20.14 ? 89   PRO C N     1 
ATOM   6057  C  CA    . PRO K  3 89  ? 43.283  28.589  133.209 1.00 20.85 ? 89   PRO C CA    1 
ATOM   6058  C  C     . PRO K  3 89  ? 43.854  29.103  131.906 1.00 22.23 ? 89   PRO C C     1 
ATOM   6059  O  O     . PRO K  3 89  ? 44.051  30.305  131.732 1.00 20.33 ? 89   PRO C O     1 
ATOM   6060  C  CB    . PRO K  3 89  ? 41.770  28.449  133.145 1.00 22.38 ? 89   PRO C CB    1 
ATOM   6061  C  CG    . PRO K  3 89  ? 41.280  29.753  133.674 1.00 21.95 ? 89   PRO C CG    1 
ATOM   6062  C  CD    . PRO K  3 89  ? 42.208  30.014  134.851 1.00 21.14 ? 89   PRO C CD    1 
ATOM   6063  N  N     . GLY K  3 90  ? 44.110  28.175  130.991 1.00 22.89 ? 90   GLY C N     1 
ATOM   6064  C  CA    . GLY K  3 90  ? 44.617  28.553  129.691 1.00 22.91 ? 90   GLY C CA    1 
ATOM   6065  C  C     . GLY K  3 90  ? 45.466  27.457  129.097 1.00 23.62 ? 90   GLY C C     1 
ATOM   6066  O  O     . GLY K  3 90  ? 45.791  26.475  129.767 1.00 24.83 ? 90   GLY C O     1 
ATOM   6067  N  N     . ASP K  3 91  ? 45.815  27.640  127.828 1.00 20.45 ? 91   ASP C N     1 
ATOM   6068  C  CA    . ASP K  3 91  ? 46.657  26.710  127.114 1.00 21.63 ? 91   ASP C CA    1 
ATOM   6069  C  C     . ASP K  3 91  ? 48.049  27.358  127.182 1.00 20.08 ? 91   ASP C C     1 
ATOM   6070  O  O     . ASP K  3 91  ? 48.437  28.170  126.338 1.00 21.45 ? 91   ASP C O     1 
ATOM   6071  C  CB    . ASP K  3 91  ? 46.136  26.574  125.681 1.00 26.73 ? 91   ASP C CB    1 
ATOM   6072  C  CG    . ASP K  3 91  ? 46.962  25.629  124.846 1.00 28.62 ? 91   ASP C CG    1 
ATOM   6073  O  OD1   . ASP K  3 91  ? 47.868  24.981  125.399 1.00 30.57 ? 91   ASP C OD1   1 
ATOM   6074  O  OD2   . ASP K  3 91  ? 46.697  25.536  123.630 1.00 32.51 ? 91   ASP C OD2   1 
ATOM   6075  N  N     . TRP K  3 92  ? 48.805  26.981  128.209 1.00 20.67 ? 92   TRP C N     1 
ATOM   6076  C  CA    . TRP K  3 92  ? 50.123  27.564  128.462 1.00 19.17 ? 92   TRP C CA    1 
ATOM   6077  C  C     . TRP K  3 92  ? 51.325  26.782  127.955 1.00 20.33 ? 92   TRP C C     1 
ATOM   6078  O  O     . TRP K  3 92  ? 51.316  25.552  127.933 1.00 21.63 ? 92   TRP C O     1 
ATOM   6079  C  CB    . TRP K  3 92  ? 50.299  27.754  129.964 1.00 19.26 ? 92   TRP C CB    1 
ATOM   6080  C  CG    . TRP K  3 92  ? 49.185  28.491  130.626 1.00 18.59 ? 92   TRP C CG    1 
ATOM   6081  C  CD1   . TRP K  3 92  ? 48.128  27.950  131.301 1.00 19.28 ? 92   TRP C CD1   1 
ATOM   6082  C  CD2   . TRP K  3 92  ? 49.018  29.913  130.685 1.00 16.76 ? 92   TRP C CD2   1 
ATOM   6083  N  NE1   . TRP K  3 92  ? 47.315  28.955  131.778 1.00 20.21 ? 92   TRP C NE1   1 
ATOM   6084  C  CE2   . TRP K  3 92  ? 47.842  30.170  131.413 1.00 17.87 ? 92   TRP C CE2   1 
ATOM   6085  C  CE3   . TRP K  3 92  ? 49.752  30.997  130.198 1.00 16.34 ? 92   TRP C CE3   1 
ATOM   6086  C  CZ2   . TRP K  3 92  ? 47.383  31.470  131.664 1.00 17.83 ? 92   TRP C CZ2   1 
ATOM   6087  C  CZ3   . TRP K  3 92  ? 49.293  32.294  130.450 1.00 18.07 ? 92   TRP C CZ3   1 
ATOM   6088  C  CH2   . TRP K  3 92  ? 48.126  32.518  131.172 1.00 17.39 ? 92   TRP C CH2   1 
ATOM   6089  N  N     . ASN K  3 93  ? 52.366  27.508  127.559 1.00 18.03 ? 93   ASN C N     1 
ATOM   6090  C  CA    . ASN K  3 93  ? 53.593  26.893  127.090 1.00 19.23 ? 93   ASN C CA    1 
ATOM   6091  C  C     . ASN K  3 93  ? 54.751  27.564  127.808 1.00 19.58 ? 93   ASN C C     1 
ATOM   6092  O  O     . ASN K  3 93  ? 54.753  28.783  127.982 1.00 20.01 ? 93   ASN C O     1 
ATOM   6093  C  CB    . ASN K  3 93  ? 53.737  27.103  125.581 1.00 26.05 ? 93   ASN C CB    1 
ATOM   6094  C  CG    . ASN K  3 93  ? 52.534  26.596  124.819 1.00 34.13 ? 93   ASN C CG    1 
ATOM   6095  O  OD1   . ASN K  3 93  ? 52.224  25.403  124.849 1.00 37.08 ? 93   ASN C OD1   1 
ATOM   6096  N  ND2   . ASN K  3 93  ? 51.829  27.505  124.151 1.00 41.13 ? 93   ASN C ND2   1 
ATOM   6097  N  N     . VAL K  3 94  ? 55.735  26.773  128.220 1.00 20.77 ? 94   VAL C N     1 
ATOM   6098  C  CA    . VAL K  3 94  ? 56.908  27.325  128.887 1.00 20.64 ? 94   VAL C CA    1 
ATOM   6099  C  C     . VAL K  3 94  ? 58.098  26.831  128.097 1.00 23.48 ? 94   VAL C C     1 
ATOM   6100  O  O     . VAL K  3 94  ? 58.240  25.626  127.866 1.00 23.82 ? 94   VAL C O     1 
ATOM   6101  C  CB    . VAL K  3 94  ? 57.031  26.826  130.352 1.00 18.47 ? 94   VAL C CB    1 
ATOM   6102  C  CG1   . VAL K  3 94  ? 58.310  27.424  131.005 1.00 19.75 ? 94   VAL C CG1   1 
ATOM   6103  C  CG2   . VAL K  3 94  ? 55.781  27.204  131.156 1.00 19.44 ? 94   VAL C CG2   1 
ATOM   6104  N  N     . LYS K  3 95  ? 58.929  27.744  127.615 1.00 21.50 ? 95   LYS C N     1 
ATOM   6105  C  CA    . LYS K  3 95  ? 60.096  27.292  126.892 1.00 24.62 ? 95   LYS C CA    1 
ATOM   6106  C  C     . LYS K  3 95  ? 61.338  28.134  127.021 1.00 21.77 ? 95   LYS C C     1 
ATOM   6107  O  O     . LYS K  3 95  ? 61.299  29.355  127.140 1.00 20.60 ? 95   LYS C O     1 
ATOM   6108  C  CB    . LYS K  3 95  ? 59.802  27.112  125.413 1.00 29.20 ? 95   LYS C CB    1 
ATOM   6109  C  CG    . LYS K  3 95  ? 59.540  28.356  124.669 1.00 30.52 ? 95   LYS C CG    1 
ATOM   6110  C  CD    . LYS K  3 95  ? 59.539  28.031  123.183 1.00 37.73 ? 95   LYS C CD    1 
ATOM   6111  C  CE    . LYS K  3 95  ? 59.058  29.196  122.347 1.00 42.74 ? 95   LYS C CE    1 
ATOM   6112  N  NZ    . LYS K  3 95  ? 58.990  28.821  120.902 1.00 42.89 ? 95   LYS C NZ    1 
ATOM   6113  N  N     . GLN K  3 96  ? 62.454  27.424  127.027 1.00 21.75 ? 96   GLN C N     1 
ATOM   6114  C  CA    . GLN K  3 96  ? 63.736  28.049  127.080 1.00 23.77 ? 96   GLN C CA    1 
ATOM   6115  C  C     . GLN K  3 96  ? 63.905  28.474  125.630 1.00 26.75 ? 96   GLN C C     1 
ATOM   6116  O  O     . GLN K  3 96  ? 63.813  27.644  124.721 1.00 30.98 ? 96   GLN C O     1 
ATOM   6117  C  CB    . GLN K  3 96  ? 64.775  27.018  127.500 1.00 25.44 ? 96   GLN C CB    1 
ATOM   6118  C  CG    . GLN K  3 96  ? 66.176  27.520  127.413 1.00 23.10 ? 96   GLN C CG    1 
ATOM   6119  C  CD    . GLN K  3 96  ? 67.186  26.440  127.723 1.00 21.61 ? 96   GLN C CD    1 
ATOM   6120  O  OE1   . GLN K  3 96  ? 66.868  25.247  127.710 1.00 24.82 ? 96   GLN C OE1   1 
ATOM   6121  N  NE2   . GLN K  3 96  ? 68.403  26.849  127.988 1.00 20.97 ? 96   GLN C NE2   1 
ATOM   6122  N  N     . VAL K  3 97  ? 64.116  29.762  125.394 1.00 25.57 ? 97   VAL C N     1 
ATOM   6123  C  CA    . VAL K  3 97  ? 64.237  30.256  124.032 1.00 30.30 ? 97   VAL C CA    1 
ATOM   6124  C  C     . VAL K  3 97  ? 65.476  29.736  123.316 1.00 37.32 ? 97   VAL C C     1 
ATOM   6125  O  O     . VAL K  3 97  ? 65.387  29.187  122.215 1.00 38.48 ? 97   VAL C O     1 
ATOM   6126  C  CB    . VAL K  3 97  ? 64.223  31.780  124.024 1.00 27.46 ? 97   VAL C CB    1 
ATOM   6127  C  CG1   . VAL K  3 97  ? 64.373  32.302  122.612 1.00 28.81 ? 97   VAL C CG1   1 
ATOM   6128  C  CG2   . VAL K  3 97  ? 62.916  32.273  124.630 1.00 27.91 ? 97   VAL C CG2   1 
ATOM   6129  N  N     . GLY K  3 98  ? 66.630  29.911  123.932 1.00 39.02 ? 98   GLY C N     1 
ATOM   6130  C  CA    . GLY K  3 98  ? 67.847  29.425  123.322 1.00 48.61 ? 98   GLY C CA    1 
ATOM   6131  C  C     . GLY K  3 98  ? 68.379  30.187  122.121 1.00 51.68 ? 98   GLY C C     1 
ATOM   6132  O  O     . GLY K  3 98  ? 68.023  31.343  121.864 1.00 54.41 ? 98   GLY C O     1 
ATOM   6133  N  N     . SER K  3 99  ? 69.245  29.495  121.385 1.00 54.97 ? 99   SER C N     1 
ATOM   6134  C  CA    . SER K  3 99  ? 69.925  30.013  120.203 1.00 55.33 ? 99   SER C CA    1 
ATOM   6135  C  C     . SER K  3 99  ? 69.097  30.729  119.142 1.00 56.14 ? 99   SER C C     1 
ATOM   6136  O  O     . SER K  3 99  ? 69.572  31.703  118.555 1.00 57.12 ? 99   SER C O     1 
ATOM   6137  C  CB    . SER K  3 99  ? 70.729  28.891  119.551 1.00 56.79 ? 99   SER C CB    1 
ATOM   6138  O  OG    . SER K  3 99  ? 72.113  29.172  119.647 1.00 60.04 ? 99   SER C OG    1 
ATOM   6139  N  N     . ARG K  3 100 ? 67.889  30.253  118.855 1.00 56.04 ? 100  ARG C N     1 
ATOM   6140  C  CA    . ARG K  3 100 ? 67.063  30.951  117.874 1.00 56.00 ? 100  ARG C CA    1 
ATOM   6141  C  C     . ARG K  3 100 ? 66.285  32.007  118.638 1.00 55.57 ? 100  ARG C C     1 
ATOM   6142  O  O     . ARG K  3 100 ? 65.062  31.968  118.774 1.00 55.39 ? 100  ARG C O     1 
ATOM   6143  C  CB    . ARG K  3 100 ? 66.144  29.986  117.133 1.00 57.84 ? 100  ARG C CB    1 
ATOM   6144  C  CG    . ARG K  3 100 ? 66.927  29.124  116.167 1.00 59.01 ? 100  ARG C CG    1 
ATOM   6145  C  CD    . ARG K  3 100 ? 66.091  28.656  115.008 1.00 60.03 ? 100  ARG C CD    1 
ATOM   6146  N  NE    . ARG K  3 100 ? 66.896  27.856  114.091 1.00 60.04 ? 100  ARG C NE    1 
ATOM   6147  C  CZ    . ARG K  3 100 ? 66.423  27.285  112.991 1.00 60.04 ? 100  ARG C CZ    1 
ATOM   6148  N  NH1   . ARG K  3 100 ? 65.140  27.428  112.670 1.00 60.04 ? 100  ARG C NH1   1 
ATOM   6149  N  NH2   . ARG K  3 100 ? 67.233  26.569  112.214 1.00 60.04 ? 100  ARG C NH2   1 
ATOM   6150  N  N     . ASN K  3 101 ? 67.081  32.947  119.129 1.00 54.13 ? 101  ASN C N     1 
ATOM   6151  C  CA    . ASN K  3 101 ? 66.701  34.088  119.942 1.00 53.34 ? 101  ASN C CA    1 
ATOM   6152  C  C     . ASN K  3 101 ? 65.967  35.239  119.251 1.00 51.29 ? 101  ASN C C     1 
ATOM   6153  O  O     . ASN K  3 101 ? 64.784  35.479  119.484 1.00 49.34 ? 101  ASN C O     1 
ATOM   6154  C  CB    . ASN K  3 101 ? 67.983  34.632  120.558 1.00 55.27 ? 101  ASN C CB    1 
ATOM   6155  C  CG    . ASN K  3 101 ? 69.170  34.507  119.615 1.00 58.76 ? 101  ASN C CG    1 
ATOM   6156  O  OD1   . ASN K  3 101 ? 69.042  34.710  118.400 1.00 57.56 ? 101  ASN C OD1   1 
ATOM   6157  N  ND2   . ASN K  3 101 ? 70.331  34.177  120.169 1.00 59.94 ? 101  ASN C ND2   1 
ATOM   6158  N  N     . ARG K  3 102 ? 66.721  35.959  118.428 1.00 49.64 ? 102  ARG C N     1 
ATOM   6159  C  CA    . ARG K  3 102 ? 66.277  37.127  117.676 1.00 48.50 ? 102  ARG C CA    1 
ATOM   6160  C  C     . ARG K  3 102 ? 64.880  37.043  117.052 1.00 48.08 ? 102  ARG C C     1 
ATOM   6161  O  O     . ARG K  3 102 ? 64.597  36.172  116.230 1.00 49.85 ? 102  ARG C O     1 
ATOM   6162  C  CB    . ARG K  3 102 ? 67.315  37.401  116.590 1.00 52.84 ? 102  ARG C CB    1 
ATOM   6163  C  CG    . ARG K  3 102 ? 67.263  38.767  115.940 1.00 56.25 ? 102  ARG C CG    1 
ATOM   6164  C  CD    . ARG K  3 102 ? 68.379  38.854  114.903 1.00 58.36 ? 102  ARG C CD    1 
ATOM   6165  N  NE    . ARG K  3 102 ? 68.451  40.148  114.231 1.00 59.31 ? 102  ARG C NE    1 
ATOM   6166  C  CZ    . ARG K  3 102 ? 69.367  40.455  113.314 1.00 60.04 ? 102  ARG C CZ    1 
ATOM   6167  N  NH1   . ARG K  3 102 ? 70.286  39.558  112.966 1.00 60.04 ? 102  ARG C NH1   1 
ATOM   6168  N  NH2   . ARG K  3 102 ? 69.366  41.655  112.737 1.00 60.04 ? 102  ARG C NH2   1 
ATOM   6169  N  N     . LEU K  3 103 ? 64.015  37.968  117.444 1.00 45.24 ? 103  LEU C N     1 
ATOM   6170  C  CA    . LEU K  3 103 ? 62.655  38.025  116.925 1.00 42.14 ? 103  LEU C CA    1 
ATOM   6171  C  C     . LEU K  3 103 ? 61.700  36.909  117.350 1.00 40.11 ? 103  LEU C C     1 
ATOM   6172  O  O     . LEU K  3 103 ? 60.576  36.847  116.844 1.00 37.51 ? 103  LEU C O     1 
ATOM   6173  C  CB    . LEU K  3 103 ? 62.669  38.129  115.396 1.00 42.46 ? 103  LEU C CB    1 
ATOM   6174  C  CG    . LEU K  3 103 ? 63.187  39.459  114.829 1.00 46.20 ? 103  LEU C CG    1 
ATOM   6175  C  CD1   . LEU K  3 103 ? 63.121  39.436  113.291 1.00 44.55 ? 103  LEU C CD1   1 
ATOM   6176  C  CD2   . LEU K  3 103 ? 62.355  40.623  115.387 1.00 42.92 ? 103  LEU C CD2   1 
ATOM   6177  N  N     . GLU K  3 104 ? 62.122  36.017  118.249 1.00 36.07 ? 104  GLU C N     1 
ATOM   6178  C  CA    . GLU K  3 104 ? 61.186  34.986  118.727 1.00 30.54 ? 104  GLU C CA    1 
ATOM   6179  C  C     . GLU K  3 104 ? 60.093  35.791  119.429 1.00 24.36 ? 104  GLU C C     1 
ATOM   6180  O  O     . GLU K  3 104 ? 58.915  35.444  119.394 1.00 26.23 ? 104  GLU C O     1 
ATOM   6181  C  CB    . GLU K  3 104 ? 61.855  34.031  119.732 1.00 34.16 ? 104  GLU C CB    1 
ATOM   6182  C  CG    . GLU K  3 104 ? 60.886  33.167  120.581 1.00 33.48 ? 104  GLU C CG    1 
ATOM   6183  C  CD    . GLU K  3 104 ? 60.109  32.125  119.781 1.00 40.67 ? 104  GLU C CD    1 
ATOM   6184  O  OE1   . GLU K  3 104 ? 60.503  31.838  118.630 1.00 44.90 ? 104  GLU C OE1   1 
ATOM   6185  O  OE2   . GLU K  3 104 ? 59.108  31.577  120.307 1.00 40.13 ? 104  GLU C OE2   1 
ATOM   6186  N  N     . ILE K  3 105 ? 60.510  36.889  120.048 1.00 25.49 ? 105  ILE C N     1 
ATOM   6187  C  CA    . ILE K  3 105 ? 59.607  37.778  120.775 1.00 26.20 ? 105  ILE C CA    1 
ATOM   6188  C  C     . ILE K  3 105 ? 58.472  38.314  119.888 1.00 25.20 ? 105  ILE C C     1 
ATOM   6189  O  O     . ILE K  3 105 ? 57.341  38.514  120.348 1.00 22.30 ? 105  ILE C O     1 
ATOM   6190  C  CB    . ILE K  3 105 ? 60.421  38.969  121.378 1.00 27.92 ? 105  ILE C CB    1 
ATOM   6191  C  CG1   . ILE K  3 105 ? 59.534  39.834  122.257 1.00 29.18 ? 105  ILE C CG1   1 
ATOM   6192  C  CG2   . ILE K  3 105 ? 61.021  39.832  120.274 1.00 32.55 ? 105  ILE C CG2   1 
ATOM   6193  C  CD1   . ILE K  3 105 ? 59.218  39.194  123.557 1.00 33.58 ? 105  ILE C CD1   1 
ATOM   6194  N  N     . ALA K  3 106 ? 58.781  38.508  118.604 1.00 26.72 ? 106  ALA C N     1 
ATOM   6195  C  CA    . ALA K  3 106 ? 57.814  39.034  117.641 1.00 25.78 ? 106  ALA C CA    1 
ATOM   6196  C  C     . ALA K  3 106 ? 56.758  38.036  117.211 1.00 26.84 ? 106  ALA C C     1 
ATOM   6197  O  O     . ALA K  3 106 ? 55.860  38.369  116.430 1.00 28.83 ? 106  ALA C O     1 
ATOM   6198  C  CB    . ALA K  3 106 ? 58.552  39.592  116.408 1.00 28.81 ? 106  ALA C CB    1 
ATOM   6199  N  N     . ARG K  3 107 ? 56.851  36.804  117.708 1.00 25.43 ? 107  ARG C N     1 
ATOM   6200  C  CA    . ARG K  3 107 ? 55.845  35.814  117.385 1.00 28.96 ? 107  ARG C CA    1 
ATOM   6201  C  C     . ARG K  3 107 ? 54.670  36.053  118.307 1.00 28.15 ? 107  ARG C C     1 
ATOM   6202  O  O     . ARG K  3 107 ? 53.591  35.467  118.128 1.00 29.12 ? 107  ARG C O     1 
ATOM   6203  C  CB    . ARG K  3 107 ? 56.364  34.412  117.625 1.00 31.51 ? 107  ARG C CB    1 
ATOM   6204  C  CG    . ARG K  3 107 ? 57.480  33.999  116.704 1.00 39.82 ? 107  ARG C CG    1 
ATOM   6205  C  CD    . ARG K  3 107 ? 57.832  32.554  116.975 1.00 44.75 ? 107  ARG C CD    1 
ATOM   6206  N  NE    . ARG K  3 107 ? 58.803  32.042  116.020 1.00 52.04 ? 107  ARG C NE    1 
ATOM   6207  C  CZ    . ARG K  3 107 ? 59.258  30.796  116.027 1.00 55.10 ? 107  ARG C CZ    1 
ATOM   6208  N  NH1   . ARG K  3 107 ? 58.823  29.940  116.945 1.00 56.64 ? 107  ARG C NH1   1 
ATOM   6209  N  NH2   . ARG K  3 107 ? 60.149  30.409  115.120 1.00 58.57 ? 107  ARG C NH2   1 
ATOM   6210  N  N     . TYR K  3 108 ? 54.880  36.912  119.307 1.00 23.55 ? 108  TYR C N     1 
ATOM   6211  C  CA    . TYR K  3 108 ? 53.827  37.183  120.253 1.00 22.93 ? 108  TYR C CA    1 
ATOM   6212  C  C     . TYR K  3 108 ? 53.161  38.506  120.041 1.00 19.86 ? 108  TYR C C     1 
ATOM   6213  O  O     . TYR K  3 108 ? 53.794  39.497  119.670 1.00 22.55 ? 108  TYR C O     1 
ATOM   6214  C  CB    . TYR K  3 108 ? 54.358  37.009  121.680 1.00 22.60 ? 108  TYR C CB    1 
ATOM   6215  C  CG    . TYR K  3 108 ? 54.949  35.625  121.789 1.00 23.21 ? 108  TYR C CG    1 
ATOM   6216  C  CD1   . TYR K  3 108 ? 56.321  35.429  121.724 1.00 23.27 ? 108  TYR C CD1   1 
ATOM   6217  C  CD2   . TYR K  3 108 ? 54.116  34.496  121.748 1.00 24.84 ? 108  TYR C CD2   1 
ATOM   6218  C  CE1   . TYR K  3 108 ? 56.863  34.138  121.601 1.00 28.45 ? 108  TYR C CE1   1 
ATOM   6219  C  CE2   . TYR K  3 108 ? 54.639  33.216  121.616 1.00 27.67 ? 108  TYR C CE2   1 
ATOM   6220  C  CZ    . TYR K  3 108 ? 56.009  33.041  121.537 1.00 26.06 ? 108  TYR C CZ    1 
ATOM   6221  O  OH    . TYR K  3 108 ? 56.519  31.776  121.343 1.00 31.25 ? 108  TYR C OH    1 
ATOM   6222  N  N     . GLN K  3 109 ? 51.868  38.482  120.301 1.00 22.15 ? 109  GLN C N     1 
ATOM   6223  C  CA    . GLN K  3 109 ? 50.979  39.592  120.078 1.00 25.32 ? 109  GLN C CA    1 
ATOM   6224  C  C     . GLN K  3 109 ? 51.463  40.964  120.487 1.00 22.38 ? 109  GLN C C     1 
ATOM   6225  O  O     . GLN K  3 109 ? 51.448  41.890  119.671 1.00 22.79 ? 109  GLN C O     1 
ATOM   6226  C  CB    . GLN K  3 109 ? 49.641  39.299  120.738 1.00 29.62 ? 109  GLN C CB    1 
ATOM   6227  C  CG    . GLN K  3 109 ? 48.456  39.523  119.819 1.00 37.81 ? 109  GLN C CG    1 
ATOM   6228  C  CD    . GLN K  3 109 ? 47.140  39.258  120.514 1.00 42.92 ? 109  GLN C CD    1 
ATOM   6229  O  OE1   . GLN K  3 109 ? 46.651  40.097  121.273 1.00 47.09 ? 109  GLN C OE1   1 
ATOM   6230  N  NE2   . GLN K  3 109 ? 46.564  38.080  120.272 1.00 40.49 ? 109  GLN C NE2   1 
ATOM   6231  N  N     . GLN K  3 110 ? 51.915  41.116  121.733 1.00 21.54 ? 110  GLN C N     1 
ATOM   6232  C  CA    . GLN K  3 110 ? 52.334  42.438  122.158 1.00 19.30 ? 110  GLN C CA    1 
ATOM   6233  C  C     . GLN K  3 110 ? 53.556  43.009  121.485 1.00 15.97 ? 110  GLN C C     1 
ATOM   6234  O  O     . GLN K  3 110 ? 53.803  44.213  121.597 1.00 18.91 ? 110  GLN C O     1 
ATOM   6235  C  CB    . GLN K  3 110 ? 52.568  42.500  123.678 1.00 16.33 ? 110  GLN C CB    1 
ATOM   6236  C  CG    . GLN K  3 110 ? 51.452  41.915  124.538 1.00 20.12 ? 110  GLN C CG    1 
ATOM   6237  C  CD    . GLN K  3 110 ? 51.791  40.534  125.005 1.00 24.03 ? 110  GLN C CD    1 
ATOM   6238  O  OE1   . GLN K  3 110 ? 51.975  39.623  124.193 1.00 19.15 ? 110  GLN C OE1   1 
ATOM   6239  N  NE2   . GLN K  3 110 ? 51.918  40.363  126.326 1.00 23.87 ? 110  GLN C NE2   1 
ATOM   6240  N  N     . TYR K  3 111 ? 54.322  42.181  120.765 1.00 17.49 ? 111  TYR C N     1 
ATOM   6241  C  CA    . TYR K  3 111 ? 55.556  42.652  120.157 1.00 18.01 ? 111  TYR C CA    1 
ATOM   6242  C  C     . TYR K  3 111 ? 55.714  42.321  118.661 1.00 19.41 ? 111  TYR C C     1 
ATOM   6243  O  O     . TYR K  3 111 ? 56.803  42.509  118.098 1.00 21.80 ? 111  TYR C O     1 
ATOM   6244  C  CB    . TYR K  3 111 ? 56.751  42.060  120.912 1.00 18.98 ? 111  TYR C CB    1 
ATOM   6245  C  CG    . TYR K  3 111 ? 56.757  42.468  122.373 1.00 16.84 ? 111  TYR C CG    1 
ATOM   6246  C  CD1   . TYR K  3 111 ? 56.246  41.606  123.361 1.00 17.45 ? 111  TYR C CD1   1 
ATOM   6247  C  CD2   . TYR K  3 111 ? 57.163  43.742  122.739 1.00 14.92 ? 111  TYR C CD2   1 
ATOM   6248  C  CE1   . TYR K  3 111 ? 56.131  42.023  124.687 1.00 18.66 ? 111  TYR C CE1   1 
ATOM   6249  C  CE2   . TYR K  3 111 ? 57.053  44.185  124.078 1.00 17.32 ? 111  TYR C CE2   1 
ATOM   6250  C  CZ    . TYR K  3 111 ? 56.530  43.309  125.035 1.00 18.37 ? 111  TYR C CZ    1 
ATOM   6251  O  OH    . TYR K  3 111 ? 56.366  43.743  126.339 1.00 16.81 ? 111  TYR C OH    1 
ATOM   6252  N  N     . ALA K  3 112 ? 54.624  41.868  118.052 1.00 22.02 ? 112  ALA C N     1 
ATOM   6253  C  CA    . ALA K  3 112 ? 54.622  41.445  116.642 1.00 21.96 ? 112  ALA C CA    1 
ATOM   6254  C  C     . ALA K  3 112 ? 55.105  42.533  115.672 1.00 24.51 ? 112  ALA C C     1 
ATOM   6255  O  O     . ALA K  3 112 ? 55.732  42.247  114.637 1.00 25.20 ? 112  ALA C O     1 
ATOM   6256  C  CB    . ALA K  3 112 ? 53.230  41.000  116.269 1.00 23.10 ? 112  ALA C CB    1 
ATOM   6257  N  N     . HIS K  3 113 ? 54.804  43.778  116.007 1.00 21.81 ? 113  HIS C N     1 
ATOM   6258  C  CA    . HIS K  3 113 ? 55.197  44.908  115.177 1.00 21.57 ? 113  HIS C CA    1 
ATOM   6259  C  C     . HIS K  3 113 ? 56.707  45.084  115.062 1.00 22.61 ? 113  HIS C C     1 
ATOM   6260  O  O     . HIS K  3 113 ? 57.196  45.785  114.176 1.00 25.49 ? 113  HIS C O     1 
ATOM   6261  C  CB    . HIS K  3 113 ? 54.558  46.189  115.707 1.00 20.77 ? 113  HIS C CB    1 
ATOM   6262  C  CG    . HIS K  3 113 ? 54.898  46.490  117.139 1.00 20.35 ? 113  HIS C CG    1 
ATOM   6263  N  ND1   . HIS K  3 113 ? 54.417  45.739  118.189 1.00 21.94 ? 113  HIS C ND1   1 
ATOM   6264  C  CD2   . HIS K  3 113 ? 55.662  47.464  117.690 1.00 22.40 ? 113  HIS C CD2   1 
ATOM   6265  C  CE1   . HIS K  3 113 ? 54.869  46.236  119.328 1.00 20.12 ? 113  HIS C CE1   1 
ATOM   6266  N  NE2   . HIS K  3 113 ? 55.627  47.282  119.054 1.00 21.32 ? 113  HIS C NE2   1 
ATOM   6267  N  N     . LEU K  3 114 ? 57.465  44.446  115.951 1.00 21.58 ? 114  LEU C N     1 
ATOM   6268  C  CA    . LEU K  3 114 ? 58.908  44.569  115.886 1.00 24.48 ? 114  LEU C CA    1 
ATOM   6269  C  C     . LEU K  3 114 ? 59.447  43.992  114.569 1.00 23.82 ? 114  LEU C C     1 
ATOM   6270  O  O     . LEU K  3 114 ? 60.466  44.443  114.064 1.00 26.53 ? 114  LEU C O     1 
ATOM   6271  C  CB    . LEU K  3 114 ? 59.547  43.864  117.092 1.00 28.68 ? 114  LEU C CB    1 
ATOM   6272  C  CG    . LEU K  3 114 ? 59.141  44.499  118.424 1.00 27.86 ? 114  LEU C CG    1 
ATOM   6273  C  CD1   . LEU K  3 114 ? 59.940  43.856  119.559 1.00 34.09 ? 114  LEU C CD1   1 
ATOM   6274  C  CD2   . LEU K  3 114 ? 59.404  45.985  118.386 1.00 32.03 ? 114  LEU C CD2   1 
ATOM   6275  N  N     . THR K  3 115 ? 58.754  43.000  114.014 1.00 27.17 ? 115  THR C N     1 
ATOM   6276  C  CA    . THR K  3 115 ? 59.161  42.388  112.739 1.00 25.67 ? 115  THR C CA    1 
ATOM   6277  C  C     . THR K  3 115 ? 59.075  43.420  111.610 1.00 25.34 ? 115  THR C C     1 
ATOM   6278  O  O     . THR K  3 115 ? 59.974  43.495  110.768 1.00 26.60 ? 115  THR C O     1 
ATOM   6279  C  CB    . THR K  3 115 ? 58.258  41.182  112.407 1.00 27.69 ? 115  THR C CB    1 
ATOM   6280  O  OG1   . THR K  3 115 ? 58.517  40.134  113.348 1.00 28.46 ? 115  THR C OG1   1 
ATOM   6281  C  CG2   . THR K  3 115 ? 58.528  40.657  110.989 1.00 31.37 ? 115  THR C CG2   1 
ATOM   6282  N  N     . ALA K  3 116 ? 57.997  44.201  111.602 1.00 26.66 ? 116  ALA C N     1 
ATOM   6283  C  CA    . ALA K  3 116 ? 57.805  45.240  110.590 1.00 28.90 ? 116  ALA C CA    1 
ATOM   6284  C  C     . ALA K  3 116 ? 58.924  46.274  110.699 1.00 30.18 ? 116  ALA C C     1 
ATOM   6285  O  O     . ALA K  3 116 ? 59.493  46.697  109.690 1.00 31.47 ? 116  ALA C O     1 
ATOM   6286  C  CB    . ALA K  3 116 ? 56.461  45.927  110.771 1.00 26.52 ? 116  ALA C CB    1 
ATOM   6287  N  N     . LEU K  3 117 ? 59.221  46.692  111.925 1.00 27.29 ? 117  LEU C N     1 
ATOM   6288  C  CA    . LEU K  3 117 ? 60.280  47.669  112.142 1.00 30.92 ? 117  LEU C CA    1 
ATOM   6289  C  C     . LEU K  3 117 ? 61.601  47.126  111.604 1.00 29.51 ? 117  LEU C C     1 
ATOM   6290  O  O     . LEU K  3 117 ? 62.333  47.838  110.917 1.00 32.23 ? 117  LEU C O     1 
ATOM   6291  C  CB    . LEU K  3 117 ? 60.419  47.993  113.635 1.00 32.00 ? 117  LEU C CB    1 
ATOM   6292  C  CG    . LEU K  3 117 ? 59.243  48.668  114.344 1.00 36.36 ? 117  LEU C CG    1 
ATOM   6293  C  CD1   . LEU K  3 117 ? 59.605  48.889  115.803 1.00 37.96 ? 117  LEU C CD1   1 
ATOM   6294  C  CD2   . LEU K  3 117 ? 58.917  49.991  113.666 1.00 41.25 ? 117  LEU C CD2   1 
ATOM   6295  N  N     . ALA K  3 118 ? 61.901  45.861  111.898 1.00 28.03 ? 118  ALA C N     1 
ATOM   6296  C  CA    . ALA K  3 118 ? 63.144  45.250  111.433 1.00 29.18 ? 118  ALA C CA    1 
ATOM   6297  C  C     . ALA K  3 118 ? 63.213  45.175  109.900 1.00 29.46 ? 118  ALA C C     1 
ATOM   6298  O  O     . ALA K  3 118 ? 64.245  45.483  109.299 1.00 29.47 ? 118  ALA C O     1 
ATOM   6299  C  CB    . ALA K  3 118 ? 63.305  43.860  112.053 1.00 27.34 ? 118  ALA C CB    1 
ATOM   6300  N  N     . LYS K  3 119 ? 62.110  44.786  109.266 1.00 30.46 ? 119  LYS C N     1 
ATOM   6301  C  CA    . LYS K  3 119 ? 62.074  44.693  107.805 1.00 34.11 ? 119  LYS C CA    1 
ATOM   6302  C  C     . LYS K  3 119 ? 62.279  46.054  107.155 1.00 33.75 ? 119  LYS C C     1 
ATOM   6303  O  O     . LYS K  3 119 ? 63.045  46.187  106.200 1.00 34.09 ? 119  LYS C O     1 
ATOM   6304  C  CB    . LYS K  3 119 ? 60.738  44.111  107.327 1.00 38.10 ? 119  LYS C CB    1 
ATOM   6305  C  CG    . LYS K  3 119 ? 60.629  42.593  107.477 1.00 44.88 ? 119  LYS C CG    1 
ATOM   6306  C  CD    . LYS K  3 119 ? 59.302  42.082  106.937 1.00 48.32 ? 119  LYS C CD    1 
ATOM   6307  C  CE    . LYS K  3 119 ? 59.182  40.570  107.100 1.00 51.34 ? 119  LYS C CE    1 
ATOM   6308  N  NZ    . LYS K  3 119 ? 57.900  40.060  106.538 1.00 54.22 ? 119  LYS C NZ    1 
ATOM   6309  N  N     . ALA K  3 120 ? 61.585  47.059  107.669 1.00 32.97 ? 120  ALA C N     1 
ATOM   6310  C  CA    . ALA K  3 120 ? 61.699  48.400  107.128 1.00 36.87 ? 120  ALA C CA    1 
ATOM   6311  C  C     . ALA K  3 120 ? 63.157  48.851  107.172 1.00 40.28 ? 120  ALA C C     1 
ATOM   6312  O  O     . ALA K  3 120 ? 63.716  49.295  106.162 1.00 41.59 ? 120  ALA C O     1 
ATOM   6313  C  CB    . ALA K  3 120 ? 60.837  49.345  107.921 1.00 32.42 ? 120  ALA C CB    1 
ATOM   6314  N  N     . ALA K  3 121 ? 63.767  48.730  108.345 1.00 40.45 ? 121  ALA C N     1 
ATOM   6315  C  CA    . ALA K  3 121 ? 65.158  49.123  108.527 1.00 45.01 ? 121  ALA C CA    1 
ATOM   6316  C  C     . ALA K  3 121 ? 66.073  48.372  107.571 1.00 46.34 ? 121  ALA C C     1 
ATOM   6317  O  O     . ALA K  3 121 ? 67.040  48.929  107.070 1.00 46.27 ? 121  ALA C O     1 
ATOM   6318  C  CB    . ALA K  3 121 ? 65.593  48.875  109.975 1.00 40.64 ? 121  ALA C CB    1 
ATOM   6319  N  N     . GLU K  3 122 ? 65.773  47.107  107.307 1.00 48.56 ? 122  GLU C N     1 
ATOM   6320  C  CA    . GLU K  3 122 ? 66.615  46.326  106.410 1.00 52.07 ? 122  GLU C CA    1 
ATOM   6321  C  C     . GLU K  3 122 ? 66.635  46.904  104.999 1.00 53.43 ? 122  GLU C C     1 
ATOM   6322  O  O     . GLU K  3 122 ? 67.678  46.950  104.355 1.00 55.24 ? 122  GLU C O     1 
ATOM   6323  C  CB    . GLU K  3 122 ? 66.138  44.873  106.348 1.00 54.27 ? 122  GLU C CB    1 
ATOM   6324  C  CG    . GLU K  3 122 ? 66.107  44.147  107.694 1.00 60.01 ? 122  GLU C CG    1 
ATOM   6325  C  CD    . GLU K  3 122 ? 67.465  44.094  108.391 1.00 60.04 ? 122  GLU C CD    1 
ATOM   6326  O  OE1   . GLU K  3 122 ? 68.477  44.537  107.792 1.00 60.04 ? 122  GLU C OE1   1 
ATOM   6327  O  OE2   . GLU K  3 122 ? 67.516  43.600  109.545 1.00 60.04 ? 122  GLU C OE2   1 
ATOM   6328  N  N     . GLU K  3 123 ? 65.480  47.350  104.524 1.00 55.17 ? 123  GLU C N     1 
ATOM   6329  C  CA    . GLU K  3 123 ? 65.375  47.904  103.179 1.00 57.73 ? 123  GLU C CA    1 
ATOM   6330  C  C     . GLU K  3 123 ? 65.963  49.322  103.061 1.00 59.00 ? 123  GLU C C     1 
ATOM   6331  O  O     . GLU K  3 123 ? 66.275  49.768  101.951 1.00 60.04 ? 123  GLU C O     1 
ATOM   6332  C  CB    . GLU K  3 123 ? 63.904  47.895  102.742 1.00 58.07 ? 123  GLU C CB    1 
ATOM   6333  C  CG    . GLU K  3 123 ? 63.660  48.270  101.279 1.00 60.03 ? 123  GLU C CG    1 
ATOM   6334  C  CD    . GLU K  3 123 ? 62.176  48.304  100.917 1.00 60.04 ? 123  GLU C CD    1 
ATOM   6335  O  OE1   . GLU K  3 123 ? 61.424  49.069  101.567 1.00 60.04 ? 123  GLU C OE1   1 
ATOM   6336  O  OE2   . GLU K  3 123 ? 61.761  47.570  99.986  1.00 60.04 ? 123  GLU C OE2   1 
ATOM   6337  N  N     . ASN K  3 124 ? 66.136  50.009  104.197 1.00 58.43 ? 124  ASN C N     1 
ATOM   6338  C  CA    . ASN K  3 124 ? 66.660  51.385  104.244 1.00 58.62 ? 124  ASN C CA    1 
ATOM   6339  C  C     . ASN K  3 124 ? 67.678  51.589  105.398 1.00 59.56 ? 124  ASN C C     1 
ATOM   6340  O  O     . ASN K  3 124 ? 67.653  50.855  106.372 1.00 60.04 ? 124  ASN C O     1 
ATOM   6341  C  CB    . ASN K  3 124 ? 65.481  52.344  104.414 1.00 60.04 ? 124  ASN C CB    1 
ATOM   6342  C  CG    . ASN K  3 124 ? 65.517  53.505  103.434 1.00 60.03 ? 124  ASN C CG    1 
ATOM   6343  O  OD1   . ASN K  3 124 ? 66.387  53.578  102.568 1.00 60.03 ? 124  ASN C OD1   1 
ATOM   6344  N  ND2   . ASN K  3 124 ? 64.560  54.419  103.568 1.00 59.89 ? 124  ASN C ND2   1 
ATOM   6345  N  N     . PRO K  3 125 ? 68.566  52.610  105.313 1.00 60.04 ? 125  PRO C N     1 
ATOM   6346  C  CA    . PRO K  3 125 ? 69.629  52.995  106.262 1.00 58.95 ? 125  PRO C CA    1 
ATOM   6347  C  C     . PRO K  3 125 ? 69.438  53.135  107.788 1.00 58.91 ? 125  PRO C C     1 
ATOM   6348  O  O     . PRO K  3 125 ? 69.211  52.149  108.501 1.00 60.04 ? 125  PRO C O     1 
ATOM   6349  C  CB    . PRO K  3 125 ? 70.153  54.295  105.664 1.00 58.76 ? 125  PRO C CB    1 
ATOM   6350  C  CG    . PRO K  3 125 ? 68.957  54.847  104.983 1.00 57.97 ? 125  PRO C CG    1 
ATOM   6351  C  CD    . PRO K  3 125 ? 68.496  53.628  104.251 1.00 60.04 ? 125  PRO C CD    1 
ATOM   6352  N  N     . GLU K  3 126 ? 69.555  54.370  108.277 1.00 59.18 ? 126  GLU C N     1 
ATOM   6353  C  CA    . GLU K  3 126 ? 69.468  54.663  109.707 1.00 57.92 ? 126  GLU C CA    1 
ATOM   6354  C  C     . GLU K  3 126 ? 68.384  53.986  110.505 1.00 58.66 ? 126  GLU C C     1 
ATOM   6355  O  O     . GLU K  3 126 ? 68.729  53.135  111.307 1.00 55.52 ? 126  GLU C O     1 
ATOM   6356  C  CB    . GLU K  3 126 ? 69.411  56.187  109.976 1.00 59.98 ? 126  GLU C CB    1 
ATOM   6357  C  CG    . GLU K  3 126 ? 68.033  56.785  110.269 1.00 58.21 ? 126  GLU C CG    1 
ATOM   6358  C  CD    . GLU K  3 126 ? 67.778  57.029  111.752 1.00 58.45 ? 126  GLU C CD    1 
ATOM   6359  O  OE1   . GLU K  3 126 ? 68.484  57.875  112.353 1.00 53.29 ? 126  GLU C OE1   1 
ATOM   6360  O  OE2   . GLU K  3 126 ? 66.869  56.376  112.316 1.00 56.86 ? 126  GLU C OE2   1 
ATOM   6361  N  N     . LEU K  3 127 ? 67.105  54.336  110.274 1.00 56.58 ? 127  LEU C N     1 
ATOM   6362  C  CA    . LEU K  3 127 ? 65.976  53.798  111.049 1.00 53.91 ? 127  LEU C CA    1 
ATOM   6363  C  C     . LEU K  3 127 ? 66.443  52.971  112.244 1.00 52.22 ? 127  LEU C C     1 
ATOM   6364  O  O     . LEU K  3 127 ? 66.029  53.226  113.380 1.00 50.27 ? 127  LEU C O     1 
ATOM   6365  C  CB    . LEU K  3 127 ? 65.009  52.985  110.175 1.00 56.01 ? 127  LEU C CB    1 
ATOM   6366  C  CG    . LEU K  3 127 ? 63.893  53.790  109.484 1.00 58.43 ? 127  LEU C CG    1 
ATOM   6367  C  CD1   . LEU K  3 127 ? 62.744  52.867  109.067 1.00 56.64 ? 127  LEU C CD1   1 
ATOM   6368  C  CD2   . LEU K  3 127 ? 63.366  54.844  110.439 1.00 58.71 ? 127  LEU C CD2   1 
ATOM   6369  N  N     . ALA K  3 128 ? 67.301  51.985  111.976 1.00 50.65 ? 128  ALA C N     1 
ATOM   6370  C  CA    . ALA K  3 128 ? 67.889  51.146  113.021 1.00 48.65 ? 128  ALA C CA    1 
ATOM   6371  C  C     . ALA K  3 128 ? 68.800  52.013  113.918 1.00 46.48 ? 128  ALA C C     1 
ATOM   6372  O  O     . ALA K  3 128 ? 69.008  51.696  115.090 1.00 45.49 ? 128  ALA C O     1 
ATOM   6373  C  CB    . ALA K  3 128 ? 68.695  50.004  112.388 1.00 49.60 ? 128  ALA C CB    1 
ATOM   6374  N  N     . ALA K  3 129 ? 69.334  53.105  113.367 1.00 44.42 ? 129  ALA C N     1 
ATOM   6375  C  CA    . ALA K  3 129 ? 70.185  53.997  114.146 1.00 44.48 ? 129  ALA C CA    1 
ATOM   6376  C  C     . ALA K  3 129 ? 69.329  54.732  115.177 1.00 45.43 ? 129  ALA C C     1 
ATOM   6377  O  O     . ALA K  3 129 ? 69.828  55.161  116.217 1.00 43.81 ? 129  ALA C O     1 
ATOM   6378  C  CB    . ALA K  3 129 ? 70.893  55.002  113.236 1.00 41.61 ? 129  ALA C CB    1 
ATOM   6379  N  N     . ALA K  3 130 ? 68.040  54.873  114.886 1.00 43.85 ? 130  ALA C N     1 
ATOM   6380  C  CA    . ALA K  3 130 ? 67.136  55.543  115.808 1.00 45.91 ? 130  ALA C CA    1 
ATOM   6381  C  C     . ALA K  3 130 ? 66.395  54.501  116.627 1.00 46.65 ? 130  ALA C C     1 
ATOM   6382  O  O     . ALA K  3 130 ? 66.346  54.566  117.861 1.00 47.44 ? 130  ALA C O     1 
ATOM   6383  C  CB    . ALA K  3 130 ? 66.135  56.400  115.030 1.00 45.71 ? 130  ALA C CB    1 
ATOM   6384  N  N     . LEU K  3 131 ? 65.828  53.532  115.922 1.00 48.67 ? 131  LEU C N     1 
ATOM   6385  C  CA    . LEU K  3 131 ? 65.051  52.467  116.537 1.00 51.64 ? 131  LEU C CA    1 
ATOM   6386  C  C     . LEU K  3 131 ? 65.914  51.484  117.318 1.00 53.18 ? 131  LEU C C     1 
ATOM   6387  O  O     . LEU K  3 131 ? 65.454  50.880  118.291 1.00 54.45 ? 131  LEU C O     1 
ATOM   6388  C  CB    . LEU K  3 131 ? 64.250  51.730  115.454 1.00 52.26 ? 131  LEU C CB    1 
ATOM   6389  C  CG    . LEU K  3 131 ? 63.464  52.646  114.498 1.00 53.61 ? 131  LEU C CG    1 
ATOM   6390  C  CD1   . LEU K  3 131 ? 62.928  51.848  113.323 1.00 54.88 ? 131  LEU C CD1   1 
ATOM   6391  C  CD2   . LEU K  3 131 ? 62.333  53.329  115.245 1.00 54.44 ? 131  LEU C CD2   1 
ATOM   6392  N  N     . GLY K  3 132 ? 67.166  51.329  116.901 1.00 52.72 ? 132  GLY C N     1 
ATOM   6393  C  CA    . GLY K  3 132 ? 68.050  50.411  117.592 1.00 52.48 ? 132  GLY C CA    1 
ATOM   6394  C  C     . GLY K  3 132 ? 67.881  48.992  117.090 1.00 53.91 ? 132  GLY C C     1 
ATOM   6395  O  O     . GLY K  3 132 ? 67.220  48.764  116.075 1.00 55.80 ? 132  GLY C O     1 
ATOM   6396  N  N     . SER K  3 133 ? 68.467  48.038  117.809 1.00 53.93 ? 133  SER C N     1 
ATOM   6397  C  CA    . SER K  3 133 ? 68.400  46.631  117.433 1.00 56.58 ? 133  SER C CA    1 
ATOM   6398  C  C     . SER K  3 133 ? 68.103  45.699  118.599 1.00 58.02 ? 133  SER C C     1 
ATOM   6399  O  O     . SER K  3 133 ? 67.682  44.557  118.390 1.00 60.04 ? 133  SER C O     1 
ATOM   6400  C  CB    . SER K  3 133 ? 69.723  46.193  116.794 1.00 56.94 ? 133  SER C CB    1 
ATOM   6401  O  OG    . SER K  3 133 ? 69.781  44.781  116.661 1.00 60.04 ? 133  SER C OG    1 
ATOM   6402  N  N     . ASP K  3 134 ? 68.318  46.178  119.821 1.00 57.47 ? 134  ASP C N     1 
ATOM   6403  C  CA    . ASP K  3 134 ? 68.110  45.338  120.994 1.00 55.42 ? 134  ASP C CA    1 
ATOM   6404  C  C     . ASP K  3 134 ? 66.653  44.962  121.256 1.00 55.92 ? 134  ASP C C     1 
ATOM   6405  O  O     . ASP K  3 134 ? 66.370  44.092  122.087 1.00 53.80 ? 134  ASP C O     1 
ATOM   6406  C  CB    . ASP K  3 134 ? 68.731  46.009  122.216 1.00 57.20 ? 134  ASP C CB    1 
ATOM   6407  C  CG    . ASP K  3 134 ? 67.743  46.785  123.028 1.00 60.03 ? 134  ASP C CG    1 
ATOM   6408  O  OD1   . ASP K  3 134 ? 66.861  47.458  122.441 1.00 60.04 ? 134  ASP C OD1   1 
ATOM   6409  O  OD2   . ASP K  3 134 ? 67.869  46.721  124.274 1.00 60.04 ? 134  ASP C OD2   1 
ATOM   6410  N  N     . TYR K  3 135 ? 65.733  45.600  120.534 1.00 54.92 ? 135  TYR C N     1 
ATOM   6411  C  CA    . TYR K  3 135 ? 64.317  45.303  120.694 1.00 54.71 ? 135  TYR C CA    1 
ATOM   6412  C  C     . TYR K  3 135 ? 63.995  43.905  120.180 1.00 55.86 ? 135  TYR C C     1 
ATOM   6413  O  O     . TYR K  3 135 ? 62.948  43.354  120.520 1.00 55.68 ? 135  TYR C O     1 
ATOM   6414  C  CB    . TYR K  3 135 ? 63.448  46.340  119.968 1.00 54.65 ? 135  TYR C CB    1 
ATOM   6415  C  CG    . TYR K  3 135 ? 63.657  46.438  118.470 1.00 52.66 ? 135  TYR C CG    1 
ATOM   6416  C  CD1   . TYR K  3 135 ? 63.418  45.346  117.631 1.00 54.62 ? 135  TYR C CD1   1 
ATOM   6417  C  CD2   . TYR K  3 135 ? 64.055  47.639  117.884 1.00 54.14 ? 135  TYR C CD2   1 
ATOM   6418  C  CE1   . TYR K  3 135 ? 63.567  45.453  116.245 1.00 54.64 ? 135  TYR C CE1   1 
ATOM   6419  C  CE2   . TYR K  3 135 ? 64.206  47.754  116.502 1.00 54.56 ? 135  TYR C CE2   1 
ATOM   6420  C  CZ    . TYR K  3 135 ? 63.961  46.661  115.691 1.00 53.78 ? 135  TYR C CZ    1 
ATOM   6421  O  OH    . TYR K  3 135 ? 64.115  46.780  114.331 1.00 54.55 ? 135  TYR C OH    1 
ATOM   6422  N  N     . THR K  3 136 ? 64.879  43.332  119.357 1.00 56.33 ? 136  THR C N     1 
ATOM   6423  C  CA    . THR K  3 136 ? 64.651  41.976  118.852 1.00 57.31 ? 136  THR C CA    1 
ATOM   6424  C  C     . THR K  3 136 ? 64.888  41.025  120.030 1.00 56.94 ? 136  THR C C     1 
ATOM   6425  O  O     . THR K  3 136 ? 65.365  39.891  119.871 1.00 57.13 ? 136  THR C O     1 
ATOM   6426  C  CB    . THR K  3 136 ? 65.588  41.625  117.657 1.00 59.33 ? 136  THR C CB    1 
ATOM   6427  O  OG1   . THR K  3 136 ? 66.958  41.850  118.019 1.00 60.04 ? 136  THR C OG1   1 
ATOM   6428  C  CG2   . THR K  3 136 ? 65.232  42.475  116.445 1.00 58.70 ? 136  THR C CG2   1 
ATOM   6429  N  N     . ILE K  3 137 ? 64.530  41.557  121.203 1.00 54.72 ? 137  ILE C N     1 
ATOM   6430  C  CA    . ILE K  3 137 ? 64.596  40.935  122.527 1.00 51.57 ? 137  ILE C CA    1 
ATOM   6431  C  C     . ILE K  3 137 ? 64.539  39.428  122.515 1.00 47.26 ? 137  ILE C C     1 
ATOM   6432  O  O     . ILE K  3 137 ? 63.737  38.837  121.797 1.00 48.22 ? 137  ILE C O     1 
ATOM   6433  C  CB    . ILE K  3 137 ? 63.411  41.391  123.415 1.00 52.81 ? 137  ILE C CB    1 
ATOM   6434  C  CG1   . ILE K  3 137 ? 63.187  42.900  123.267 1.00 52.61 ? 137  ILE C CG1   1 
ATOM   6435  C  CG2   . ILE K  3 137 ? 63.680  41.020  124.875 1.00 54.00 ? 137  ILE C CG2   1 
ATOM   6436  C  CD1   . ILE K  3 137 ? 61.945  43.413  123.964 1.00 51.20 ? 137  ILE C CD1   1 
ATOM   6437  N  N     . THR K  3 138 ? 65.376  38.813  123.336 1.00 41.72 ? 138  THR C N     1 
ATOM   6438  C  CA    . THR K  3 138 ? 65.404  37.366  123.448 1.00 39.96 ? 138  THR C CA    1 
ATOM   6439  C  C     . THR K  3 138 ? 65.418  36.988  124.929 1.00 30.09 ? 138  THR C C     1 
ATOM   6440  O  O     . THR K  3 138 ? 66.489  36.822  125.490 1.00 33.23 ? 138  THR C O     1 
ATOM   6441  C  CB    . THR K  3 138 ? 66.686  36.749  122.834 1.00 42.78 ? 138  THR C CB    1 
ATOM   6442  O  OG1   . THR K  3 138 ? 66.744  37.016  121.428 1.00 46.41 ? 138  THR C OG1   1 
ATOM   6443  C  CG2   . THR K  3 138 ? 66.696  35.243  123.078 1.00 42.15 ? 138  THR C CG2   1 
ATOM   6444  N  N     . PRO K  3 139 ? 64.245  36.871  125.570 1.00 28.18 ? 139  PRO C N     1 
ATOM   6445  C  CA    . PRO K  3 139 ? 64.266  36.498  126.997 1.00 25.26 ? 139  PRO C CA    1 
ATOM   6446  C  C     . PRO K  3 139 ? 64.849  35.085  127.131 1.00 24.35 ? 139  PRO C C     1 
ATOM   6447  O  O     . PRO K  3 139 ? 64.831  34.309  126.179 1.00 27.24 ? 139  PRO C O     1 
ATOM   6448  C  CB    . PRO K  3 139 ? 62.793  36.528  127.398 1.00 26.97 ? 139  PRO C CB    1 
ATOM   6449  C  CG    . PRO K  3 139 ? 62.163  37.512  126.372 1.00 28.29 ? 139  PRO C CG    1 
ATOM   6450  C  CD    . PRO K  3 139 ? 62.868  37.109  125.107 1.00 30.63 ? 139  PRO C CD    1 
ATOM   6451  N  N     . ASP K  3 140 ? 65.356  34.741  128.308 1.00 14.81 ? 140  ASP C N     1 
ATOM   6452  C  CA    . ASP K  3 140 ? 65.919  33.402  128.518 1.00 14.88 ? 140  ASP C CA    1 
ATOM   6453  C  C     . ASP K  3 140 ? 64.855  32.304  128.458 1.00 16.25 ? 140  ASP C C     1 
ATOM   6454  O  O     . ASP K  3 140 ? 65.044  31.264  127.817 1.00 17.23 ? 140  ASP C O     1 
ATOM   6455  C  CB    . ASP K  3 140 ? 66.602  33.332  129.880 1.00 13.64 ? 140  ASP C CB    1 
ATOM   6456  C  CG    . ASP K  3 140 ? 67.810  34.199  129.960 1.00 18.93 ? 140  ASP C CG    1 
ATOM   6457  O  OD1   . ASP K  3 140 ? 68.291  34.674  128.909 1.00 15.00 ? 140  ASP C OD1   1 
ATOM   6458  O  OD2   . ASP K  3 140 ? 68.303  34.414  131.075 1.00 14.29 ? 140  ASP C OD2   1 
ATOM   6459  N  N     . ILE K  3 141 ? 63.743  32.554  129.143 1.00 13.86 ? 141  ILE C N     1 
ATOM   6460  C  CA    . ILE K  3 141 ? 62.628  31.630  129.202 1.00 14.96 ? 141  ILE C CA    1 
ATOM   6461  C  C     . ILE K  3 141 ? 61.372  32.465  129.011 1.00 16.41 ? 141  ILE C C     1 
ATOM   6462  O  O     . ILE K  3 141 ? 61.265  33.576  129.544 1.00 15.53 ? 141  ILE C O     1 
ATOM   6463  C  CB    . ILE K  3 141 ? 62.526  30.965  130.611 1.00 15.14 ? 141  ILE C CB    1 
ATOM   6464  C  CG1   . ILE K  3 141 ? 63.751  30.086  130.895 1.00 14.94 ? 141  ILE C CG1   1 
ATOM   6465  C  CG2   . ILE K  3 141 ? 61.238  30.105  130.692 1.00 17.21 ? 141  ILE C CG2   1 
ATOM   6466  C  CD1   . ILE K  3 141 ? 63.786  29.590  132.378 1.00 16.54 ? 141  ILE C CD1   1 
ATOM   6467  N  N     . ILE K  3 142 ? 60.429  31.956  128.227 1.00 15.18 ? 142  ILE C N     1 
ATOM   6468  C  CA    . ILE K  3 142 ? 59.173  32.673  128.077 1.00 13.97 ? 142  ILE C CA    1 
ATOM   6469  C  C     . ILE K  3 142 ? 58.013  31.754  128.420 1.00 14.93 ? 142  ILE C C     1 
ATOM   6470  O  O     . ILE K  3 142 ? 58.120  30.532  128.288 1.00 18.29 ? 142  ILE C O     1 
ATOM   6471  C  CB    . ILE K  3 142 ? 58.942  33.211  126.638 1.00 16.20 ? 142  ILE C CB    1 
ATOM   6472  C  CG1   . ILE K  3 142 ? 59.029  32.074  125.615 1.00 20.07 ? 142  ILE C CG1   1 
ATOM   6473  C  CG2   . ILE K  3 142 ? 59.947  34.286  126.320 1.00 17.13 ? 142  ILE C CG2   1 
ATOM   6474  C  CD1   . ILE K  3 142 ? 58.676  32.546  124.199 1.00 24.73 ? 142  ILE C CD1   1 
ATOM   6475  N  N     . VAL K  3 143 ? 56.936  32.345  128.930 1.00 13.62 ? 143  VAL C N     1 
ATOM   6476  C  CA    . VAL K  3 143 ? 55.713  31.599  129.194 1.00 14.98 ? 143  VAL C CA    1 
ATOM   6477  C  C     . VAL K  3 143 ? 54.738  32.295  128.258 1.00 17.23 ? 143  VAL C C     1 
ATOM   6478  O  O     . VAL K  3 143 ? 54.676  33.528  128.238 1.00 15.83 ? 143  VAL C O     1 
ATOM   6479  C  CB    . VAL K  3 143 ? 55.234  31.752  130.649 1.00 16.60 ? 143  VAL C CB    1 
ATOM   6480  C  CG1   . VAL K  3 143 ? 53.908  30.988  130.852 1.00 16.49 ? 143  VAL C CG1   1 
ATOM   6481  C  CG2   . VAL K  3 143 ? 56.309  31.195  131.585 1.00 17.43 ? 143  VAL C CG2   1 
ATOM   6482  N  N     . THR K  3 144 ? 54.016  31.517  127.451 1.00 15.77 ? 144  THR C N     1 
ATOM   6483  C  CA    . THR K  3 144 ? 53.055  32.088  126.504 1.00 18.16 ? 144  THR C CA    1 
ATOM   6484  C  C     . THR K  3 144 ? 51.670  31.472  126.664 1.00 17.88 ? 144  THR C C     1 
ATOM   6485  O  O     . THR K  3 144 ? 51.515  30.363  127.210 1.00 17.47 ? 144  THR C O     1 
ATOM   6486  C  CB    . THR K  3 144 ? 53.504  31.862  125.030 1.00 19.55 ? 144  THR C CB    1 
ATOM   6487  O  OG1   . THR K  3 144 ? 53.557  30.456  124.781 1.00 19.70 ? 144  THR C OG1   1 
ATOM   6488  C  CG2   . THR K  3 144 ? 54.881  32.486  124.764 1.00 24.08 ? 144  THR C CG2   1 
ATOM   6489  N  N     . ARG K  3 145 ? 50.651  32.200  126.202 1.00 18.61 ? 145  ARG C N     1 
ATOM   6490  C  CA    . ARG K  3 145 ? 49.285  31.720  126.280 1.00 19.43 ? 145  ARG C CA    1 
ATOM   6491  C  C     . ARG K  3 145 ? 48.723  31.616  124.863 1.00 20.06 ? 145  ARG C C     1 
ATOM   6492  O  O     . ARG K  3 145 ? 48.749  32.593  124.100 1.00 19.95 ? 145  ARG C O     1 
ATOM   6493  C  CB    . ARG K  3 145 ? 48.401  32.677  127.091 1.00 20.69 ? 145  ARG C CB    1 
ATOM   6494  C  CG    . ARG K  3 145 ? 47.035  32.072  127.418 1.00 22.69 ? 145  ARG C CG    1 
ATOM   6495  C  CD    . ARG K  3 145 ? 46.115  33.027  128.163 1.00 21.96 ? 145  ARG C CD    1 
ATOM   6496  N  NE    . ARG K  3 145 ? 44.834  32.386  128.460 1.00 22.67 ? 145  ARG C NE    1 
ATOM   6497  C  CZ    . ARG K  3 145 ? 43.884  32.917  129.213 1.00 22.62 ? 145  ARG C CZ    1 
ATOM   6498  N  NH1   . ARG K  3 145 ? 44.066  34.110  129.766 1.00 23.22 ? 145  ARG C NH1   1 
ATOM   6499  N  NH2   . ARG K  3 145 ? 42.730  32.275  129.389 1.00 21.72 ? 145  ARG C NH2   1 
ATOM   6500  N  N     . ASN K  3 146 ? 48.216  30.442  124.525 1.00 19.64 ? 146  ASN C N     1 
ATOM   6501  C  CA    . ASN K  3 146 ? 47.625  30.273  123.203 1.00 22.45 ? 146  ASN C CA    1 
ATOM   6502  C  C     . ASN K  3 146 ? 46.242  30.867  123.232 1.00 22.32 ? 146  ASN C C     1 
ATOM   6503  O  O     . ASN K  3 146 ? 45.624  30.975  124.287 1.00 19.73 ? 146  ASN C O     1 
ATOM   6504  C  CB    . ASN K  3 146 ? 47.587  28.803  122.824 1.00 23.86 ? 146  ASN C CB    1 
ATOM   6505  C  CG    . ASN K  3 146 ? 48.965  28.266  122.570 1.00 31.20 ? 146  ASN C CG    1 
ATOM   6506  O  OD1   . ASN K  3 146 ? 49.782  28.920  121.907 1.00 32.72 ? 146  ASN C OD1   1 
ATOM   6507  N  ND2   . ASN K  3 146 ? 49.252  27.084  123.102 1.00 38.25 ? 146  ASN C ND2   1 
ATOM   6508  N  N     . LEU K  3 147 ? 45.742  31.245  122.063 1.00 21.29 ? 147  LEU C N     1 
ATOM   6509  C  CA    . LEU K  3 147 ? 44.441  31.871  122.003 1.00 23.94 ? 147  LEU C CA    1 
ATOM   6510  C  C     . LEU K  3 147 ? 43.280  30.893  122.160 1.00 26.21 ? 147  LEU C C     1 
ATOM   6511  O  O     . LEU K  3 147 ? 43.452  29.681  122.035 1.00 28.79 ? 147  LEU C O     1 
ATOM   6512  C  CB    . LEU K  3 147 ? 44.351  32.715  120.727 1.00 22.69 ? 147  LEU C CB    1 
ATOM   6513  C  CG    . LEU K  3 147 ? 45.567  33.640  120.561 1.00 23.75 ? 147  LEU C CG    1 
ATOM   6514  C  CD1   . LEU K  3 147 ? 45.401  34.532  119.312 1.00 23.39 ? 147  LEU C CD1   1 
ATOM   6515  C  CD2   . LEU K  3 147 ? 45.742  34.507  121.809 1.00 20.43 ? 147  LEU C CD2   1 
ATOM   6516  N  N     . ILE K  3 148 ? 42.108  31.447  122.453 1.00 25.14 ? 148  ILE C N     1 
ATOM   6517  C  CA    . ILE K  3 148 ? 40.890  30.701  122.738 1.00 27.07 ? 148  ILE C CA    1 
ATOM   6518  C  C     . ILE K  3 148 ? 39.837  30.749  121.630 1.00 29.54 ? 148  ILE C C     1 
ATOM   6519  O  O     . ILE K  3 148 ? 39.626  31.794  121.005 1.00 28.24 ? 148  ILE C O     1 
ATOM   6520  C  CB    . ILE K  3 148 ? 40.255  31.270  124.025 1.00 28.54 ? 148  ILE C CB    1 
ATOM   6521  C  CG1   . ILE K  3 148 ? 41.346  31.443  125.092 1.00 29.42 ? 148  ILE C CG1   1 
ATOM   6522  C  CG2   . ILE K  3 148 ? 39.159  30.379  124.520 1.00 30.86 ? 148  ILE C CG2   1 
ATOM   6523  C  CD1   . ILE K  3 148 ? 40.910  32.259  126.303 1.00 30.79 ? 148  ILE C CD1   1 
ATOM   6524  N  N     . ALA K  3 149 ? 39.159  29.625  121.414 1.00 30.69 ? 149  ALA C N     1 
ATOM   6525  C  CA    . ALA K  3 149 ? 38.112  29.570  120.385 1.00 30.24 ? 149  ALA C CA    1 
ATOM   6526  C  C     . ALA K  3 149 ? 36.794  30.096  120.949 1.00 28.87 ? 149  ALA C C     1 
ATOM   6527  O  O     . ALA K  3 149 ? 36.611  30.176  122.166 1.00 26.49 ? 149  ALA C O     1 
ATOM   6528  C  CB    . ALA K  3 149 ? 37.944  28.128  119.895 1.00 28.85 ? 149  ALA C CB    1 
ATOM   6529  N  N     . ASP K  3 150 ? 35.854  30.462  120.075 1.00 28.50 ? 150  ASP C N     1 
ATOM   6530  C  CA    . ASP K  3 150 ? 34.578  30.966  120.559 1.00 29.53 ? 150  ASP C CA    1 
ATOM   6531  C  C     . ASP K  3 150 ? 33.854  29.944  121.434 1.00 27.72 ? 150  ASP C C     1 
ATOM   6532  O  O     . ASP K  3 150 ? 33.171  30.301  122.394 1.00 28.34 ? 150  ASP C O     1 
ATOM   6533  C  CB    . ASP K  3 150 ? 33.674  31.374  119.385 1.00 33.06 ? 150  ASP C CB    1 
ATOM   6534  C  CG    . ASP K  3 150 ? 34.188  32.609  118.651 1.00 38.85 ? 150  ASP C CG    1 
ATOM   6535  O  OD1   . ASP K  3 150 ? 34.919  33.411  119.266 1.00 40.46 ? 150  ASP C OD1   1 
ATOM   6536  O  OD2   . ASP K  3 150 ? 33.853  32.783  117.461 1.00 44.69 ? 150  ASP C OD2   1 
ATOM   6537  N  N     . ALA K  3 151 ? 33.995  28.665  121.092 1.00 28.19 ? 151  ALA C N     1 
ATOM   6538  C  CA    . ALA K  3 151 ? 33.343  27.604  121.852 1.00 29.98 ? 151  ALA C CA    1 
ATOM   6539  C  C     . ALA K  3 151 ? 33.705  27.690  123.328 1.00 27.97 ? 151  ALA C C     1 
ATOM   6540  O  O     . ALA K  3 151 ? 32.872  27.425  124.195 1.00 31.71 ? 151  ALA C O     1 
ATOM   6541  C  CB    . ALA K  3 151 ? 33.734  26.245  121.292 1.00 29.87 ? 151  ALA C CB    1 
ATOM   6542  N  N     . GLU K  3 152 ? 34.949  28.077  123.613 1.00 28.65 ? 152  GLU C N     1 
ATOM   6543  C  CA    . GLU K  3 152 ? 35.394  28.194  125.001 1.00 26.15 ? 152  GLU C CA    1 
ATOM   6544  C  C     . GLU K  3 152 ? 34.935  29.520  125.613 1.00 24.49 ? 152  GLU C C     1 
ATOM   6545  O  O     . GLU K  3 152 ? 34.472  29.558  126.741 1.00 26.08 ? 152  GLU C O     1 
ATOM   6546  C  CB    . GLU K  3 152 ? 36.920  28.059  125.086 1.00 28.57 ? 152  GLU C CB    1 
ATOM   6547  C  CG    . GLU K  3 152 ? 37.489  28.241  126.498 1.00 35.92 ? 152  GLU C CG    1 
ATOM   6548  C  CD    . GLU K  3 152 ? 36.894  27.272  127.506 1.00 41.59 ? 152  GLU C CD    1 
ATOM   6549  O  OE1   . GLU K  3 152 ? 36.571  26.122  127.121 1.00 40.08 ? 152  GLU C OE1   1 
ATOM   6550  O  OE2   . GLU K  3 152 ? 36.760  27.653  128.692 1.00 43.28 ? 152  GLU C OE2   1 
ATOM   6551  N  N     . ILE K  3 153 ? 35.063  30.611  124.868 1.00 26.09 ? 153  ILE C N     1 
ATOM   6552  C  CA    . ILE K  3 153 ? 34.599  31.886  125.402 1.00 26.79 ? 153  ILE C CA    1 
ATOM   6553  C  C     . ILE K  3 153 ? 33.119  31.734  125.693 1.00 24.09 ? 153  ILE C C     1 
ATOM   6554  O  O     . ILE K  3 153 ? 32.633  32.208  126.703 1.00 22.28 ? 153  ILE C O     1 
ATOM   6555  C  CB    . ILE K  3 153 ? 34.814  33.037  124.397 1.00 24.12 ? 153  ILE C CB    1 
ATOM   6556  C  CG1   . ILE K  3 153 ? 36.311  33.325  124.271 1.00 26.46 ? 153  ILE C CG1   1 
ATOM   6557  C  CG2   . ILE K  3 153 ? 34.045  34.295  124.860 1.00 25.61 ? 153  ILE C CG2   1 
ATOM   6558  C  CD1   . ILE K  3 153 ? 36.683  34.255  123.134 1.00 27.72 ? 153  ILE C CD1   1 
ATOM   6559  N  N     . ASN K  3 154 ? 32.409  31.039  124.805 1.00 27.90 ? 154  ASN C N     1 
ATOM   6560  C  CA    . ASN K  3 154 ? 30.972  30.821  124.965 1.00 29.54 ? 154  ASN C CA    1 
ATOM   6561  C  C     . ASN K  3 154 ? 30.615  29.507  125.675 1.00 31.61 ? 154  ASN C C     1 
ATOM   6562  O  O     . ASN K  3 154 ? 29.522  28.978  125.495 1.00 30.15 ? 154  ASN C O     1 
ATOM   6563  C  CB    . ASN K  3 154 ? 30.283  30.840  123.595 1.00 29.67 ? 154  ASN C CB    1 
ATOM   6564  C  CG    . ASN K  3 154 ? 30.324  32.198  122.944 1.00 28.71 ? 154  ASN C CG    1 
ATOM   6565  O  OD1   . ASN K  3 154 ? 30.322  33.222  123.631 1.00 27.67 ? 154  ASN C OD1   1 
ATOM   6566  N  ND2   . ASN K  3 154 ? 30.338  32.221  121.612 1.00 25.93 ? 154  ASN C ND2   1 
ATOM   6567  N  N     . ARG K  3 155 ? 31.521  28.983  126.490 1.00 33.21 ? 155  ARG C N     1 
ATOM   6568  C  CA    . ARG K  3 155 ? 31.249  27.725  127.173 1.00 34.99 ? 155  ARG C CA    1 
ATOM   6569  C  C     . ARG K  3 155 ? 29.969  27.686  128.004 1.00 36.07 ? 155  ARG C C     1 
ATOM   6570  O  O     . ARG K  3 155 ? 29.256  26.678  127.999 1.00 36.58 ? 155  ARG C O     1 
ATOM   6571  C  CB    . ARG K  3 155 ? 32.423  27.331  128.073 1.00 38.20 ? 155  ARG C CB    1 
ATOM   6572  C  CG    . ARG K  3 155 ? 32.175  26.018  128.820 1.00 40.08 ? 155  ARG C CG    1 
ATOM   6573  C  CD    . ARG K  3 155 ? 32.889  25.989  130.158 1.00 45.46 ? 155  ARG C CD    1 
ATOM   6574  N  NE    . ARG K  3 155 ? 34.339  26.078  130.014 1.00 46.50 ? 155  ARG C NE    1 
ATOM   6575  C  CZ    . ARG K  3 155 ? 35.187  26.101  131.040 1.00 46.36 ? 155  ARG C CZ    1 
ATOM   6576  N  NH1   . ARG K  3 155 ? 34.728  26.043  132.285 1.00 47.21 ? 155  ARG C NH1   1 
ATOM   6577  N  NH2   . ARG K  3 155 ? 36.492  26.179  130.824 1.00 47.49 ? 155  ARG C NH2   1 
ATOM   6578  N  N     . ASN K  3 156 ? 29.667  28.762  128.727 1.00 33.82 ? 156  ASN C N     1 
ATOM   6579  C  CA    . ASN K  3 156 ? 28.479  28.770  129.569 1.00 35.20 ? 156  ASN C CA    1 
ATOM   6580  C  C     . ASN K  3 156 ? 27.362  29.675  129.077 1.00 35.19 ? 156  ASN C C     1 
ATOM   6581  O  O     . ASN K  3 156 ? 26.197  29.472  129.429 1.00 33.24 ? 156  ASN C O     1 
ATOM   6582  C  CB    . ASN K  3 156 ? 28.854  29.166  130.998 1.00 36.82 ? 156  ASN C CB    1 
ATOM   6583  C  CG    . ASN K  3 156 ? 29.864  28.218  131.609 1.00 41.41 ? 156  ASN C CG    1 
ATOM   6584  O  OD1   . ASN K  3 156 ? 29.673  27.002  131.589 1.00 41.40 ? 156  ASN C OD1   1 
ATOM   6585  N  ND2   . ASN K  3 156 ? 30.945  28.766  132.155 1.00 39.70 ? 156  ASN C ND2   1 
ATOM   6586  N  N     . GLU K  3 157 ? 27.722  30.674  128.278 1.00 35.38 ? 157  GLU C N     1 
ATOM   6587  C  CA    . GLU K  3 157 ? 26.755  31.634  127.745 1.00 30.96 ? 157  GLU C CA    1 
ATOM   6588  C  C     . GLU K  3 157 ? 27.150  32.048  126.337 1.00 29.46 ? 157  GLU C C     1 
ATOM   6589  O  O     . GLU K  3 157 ? 28.294  31.904  125.927 1.00 29.87 ? 157  GLU C O     1 
ATOM   6590  C  CB    . GLU K  3 157 ? 26.692  32.876  128.649 1.00 35.30 ? 157  GLU C CB    1 
ATOM   6591  C  CG    . GLU K  3 157 ? 26.159  32.615  130.059 1.00 35.72 ? 157  GLU C CG    1 
ATOM   6592  C  CD    . GLU K  3 157 ? 26.333  33.808  130.992 1.00 41.85 ? 157  GLU C CD    1 
ATOM   6593  O  OE1   . GLU K  3 157 ? 27.491  34.135  131.336 1.00 40.30 ? 157  GLU C OE1   1 
ATOM   6594  O  OE2   . GLU K  3 157 ? 25.316  34.426  131.389 1.00 39.72 ? 157  GLU C OE2   1 
ATOM   6595  N  N     . PHE K  3 158 ? 26.195  32.558  125.573 1.00 28.44 ? 158  PHE C N     1 
ATOM   6596  C  CA    . PHE K  3 158 ? 26.501  32.998  124.220 1.00 29.37 ? 158  PHE C CA    1 
ATOM   6597  C  C     . PHE K  3 158 ? 26.970  34.443  124.397 1.00 30.39 ? 158  PHE C C     1 
ATOM   6598  O  O     . PHE K  3 158 ? 26.173  35.374  124.359 1.00 33.41 ? 158  PHE C O     1 
ATOM   6599  C  CB    . PHE K  3 158 ? 25.231  32.920  123.352 1.00 29.59 ? 158  PHE C CB    1 
ATOM   6600  C  CG    . PHE K  3 158 ? 25.436  33.349  121.934 1.00 32.93 ? 158  PHE C CG    1 
ATOM   6601  C  CD1   . PHE K  3 158 ? 26.572  32.970  121.231 1.00 35.31 ? 158  PHE C CD1   1 
ATOM   6602  C  CD2   . PHE K  3 158 ? 24.470  34.108  121.283 1.00 35.54 ? 158  PHE C CD2   1 
ATOM   6603  C  CE1   . PHE K  3 158 ? 26.744  33.337  119.902 1.00 36.36 ? 158  PHE C CE1   1 
ATOM   6604  C  CE2   . PHE K  3 158 ? 24.638  34.475  119.955 1.00 34.43 ? 158  PHE C CE2   1 
ATOM   6605  C  CZ    . PHE K  3 158 ? 25.771  34.091  119.265 1.00 35.01 ? 158  PHE C CZ    1 
ATOM   6606  N  N     . LEU K  3 159 ? 28.269  34.609  124.623 1.00 28.48 ? 159  LEU C N     1 
ATOM   6607  C  CA    . LEU K  3 159 ? 28.850  35.927  124.864 1.00 29.33 ? 159  LEU C CA    1 
ATOM   6608  C  C     . LEU K  3 159 ? 29.256  36.683  123.618 1.00 26.91 ? 159  LEU C C     1 
ATOM   6609  O  O     . LEU K  3 159 ? 29.020  37.889  123.527 1.00 29.57 ? 159  LEU C O     1 
ATOM   6610  C  CB    . LEU K  3 159 ? 30.085  35.807  125.769 1.00 26.74 ? 159  LEU C CB    1 
ATOM   6611  C  CG    . LEU K  3 159 ? 29.916  35.180  127.149 1.00 28.10 ? 159  LEU C CG    1 
ATOM   6612  C  CD1   . LEU K  3 159 ? 31.281  35.218  127.872 1.00 27.04 ? 159  LEU C CD1   1 
ATOM   6613  C  CD2   . LEU K  3 159 ? 28.873  35.935  127.943 1.00 27.82 ? 159  LEU C CD2   1 
ATOM   6614  N  N     . VAL K  3 160 ? 29.869  35.985  122.664 1.00 25.47 ? 160  VAL C N     1 
ATOM   6615  C  CA    . VAL K  3 160 ? 30.345  36.631  121.451 1.00 28.40 ? 160  VAL C CA    1 
ATOM   6616  C  C     . VAL K  3 160 ? 30.038  35.913  120.148 1.00 32.30 ? 160  VAL C C     1 
ATOM   6617  O  O     . VAL K  3 160 ? 29.792  34.703  120.122 1.00 33.73 ? 160  VAL C O     1 
ATOM   6618  C  CB    . VAL K  3 160 ? 31.898  36.821  121.480 1.00 28.14 ? 160  VAL C CB    1 
ATOM   6619  C  CG1   . VAL K  3 160 ? 32.307  37.632  122.694 1.00 24.69 ? 160  VAL C CG1   1 
ATOM   6620  C  CG2   . VAL K  3 160 ? 32.603  35.457  121.523 1.00 27.53 ? 160  VAL C CG2   1 
ATOM   6621  N  N     . ASP K  3 161 ? 30.043  36.691  119.072 1.00 34.31 ? 161  ASP C N     1 
ATOM   6622  C  CA    . ASP K  3 161 ? 29.893  36.155  117.733 1.00 34.39 ? 161  ASP C CA    1 
ATOM   6623  C  C     . ASP K  3 161 ? 30.904  36.916  116.889 1.00 35.17 ? 161  ASP C C     1 
ATOM   6624  O  O     . ASP K  3 161 ? 31.801  37.583  117.434 1.00 33.89 ? 161  ASP C O     1 
ATOM   6625  C  CB    . ASP K  3 161 ? 28.451  36.266  117.182 1.00 37.73 ? 161  ASP C CB    1 
ATOM   6626  C  CG    . ASP K  3 161 ? 27.988  37.694  116.944 1.00 39.14 ? 161  ASP C CG    1 
ATOM   6627  O  OD1   . ASP K  3 161 ? 28.821  38.610  116.772 1.00 36.21 ? 161  ASP C OD1   1 
ATOM   6628  O  OD2   . ASP K  3 161 ? 26.752  37.881  116.908 1.00 42.97 ? 161  ASP C OD2   1 
ATOM   6629  N  N     . GLU K  3 162 ? 30.787  36.833  115.574 1.00 33.60 ? 162  GLU C N     1 
ATOM   6630  C  CA    . GLU K  3 162 ? 31.754  37.488  114.713 1.00 34.77 ? 162  GLU C CA    1 
ATOM   6631  C  C     . GLU K  3 162 ? 31.637  39.007  114.599 1.00 31.38 ? 162  GLU C C     1 
ATOM   6632  O  O     . GLU K  3 162 ? 32.502  39.640  114.000 1.00 33.62 ? 162  GLU C O     1 
ATOM   6633  C  CB    . GLU K  3 162 ? 31.693  36.882  113.308 1.00 39.37 ? 162  GLU C CB    1 
ATOM   6634  C  CG    . GLU K  3 162 ? 30.363  37.118  112.588 1.00 46.10 ? 162  GLU C CG    1 
ATOM   6635  C  CD    . GLU K  3 162 ? 29.377  35.983  112.781 1.00 49.52 ? 162  GLU C CD    1 
ATOM   6636  O  OE1   . GLU K  3 162 ? 29.226  35.490  113.919 1.00 49.38 ? 162  GLU C OE1   1 
ATOM   6637  O  OE2   . GLU K  3 162 ? 28.739  35.584  111.784 1.00 55.57 ? 162  GLU C OE2   1 
ATOM   6638  N  N     . ASN K  3 163 ? 30.596  39.594  115.177 1.00 31.37 ? 163  ASN C N     1 
ATOM   6639  C  CA    . ASN K  3 163 ? 30.420  41.038  115.042 1.00 30.75 ? 163  ASN C CA    1 
ATOM   6640  C  C     . ASN K  3 163 ? 30.573  41.881  116.298 1.00 32.55 ? 163  ASN C C     1 
ATOM   6641  O  O     . ASN K  3 163 ? 30.206  43.049  116.313 1.00 34.15 ? 163  ASN C O     1 
ATOM   6642  C  CB    . ASN K  3 163 ? 29.066  41.308  114.396 1.00 32.05 ? 163  ASN C CB    1 
ATOM   6643  C  CG    . ASN K  3 163 ? 28.993  40.747  112.984 1.00 33.64 ? 163  ASN C CG    1 
ATOM   6644  O  OD1   . ASN K  3 163 ? 29.848  41.049  112.151 1.00 37.05 ? 163  ASN C OD1   1 
ATOM   6645  N  ND2   . ASN K  3 163 ? 27.984  39.928  112.714 1.00 35.41 ? 163  ASN C ND2   1 
ATOM   6646  N  N     . ILE K  3 164 ? 31.127  41.290  117.346 1.00 27.38 ? 164  ILE C N     1 
ATOM   6647  C  CA    . ILE K  3 164 ? 31.320  41.997  118.608 1.00 26.45 ? 164  ILE C CA    1 
ATOM   6648  C  C     . ILE K  3 164 ? 32.696  41.567  119.160 1.00 25.50 ? 164  ILE C C     1 
ATOM   6649  O  O     . ILE K  3 164 ? 33.153  40.460  118.871 1.00 25.18 ? 164  ILE C O     1 
ATOM   6650  C  CB    . ILE K  3 164 ? 30.182  41.625  119.583 1.00 25.25 ? 164  ILE C CB    1 
ATOM   6651  C  CG1   . ILE K  3 164 ? 30.206  42.526  120.830 1.00 27.33 ? 164  ILE C CG1   1 
ATOM   6652  C  CG2   . ILE K  3 164 ? 30.277  40.143  119.954 1.00 24.98 ? 164  ILE C CG2   1 
ATOM   6653  C  CD1   . ILE K  3 164 ? 29.943  44.003  120.543 1.00 24.66 ? 164  ILE C CD1   1 
ATOM   6654  N  N     . ALA K  3 165 ? 33.373  42.454  119.897 1.00 25.85 ? 165  ALA C N     1 
ATOM   6655  C  CA    . ALA K  3 165 ? 34.688  42.114  120.484 1.00 23.20 ? 165  ALA C CA    1 
ATOM   6656  C  C     . ALA K  3 165 ? 35.577  41.483  119.425 1.00 22.29 ? 165  ALA C C     1 
ATOM   6657  O  O     . ALA K  3 165 ? 36.233  40.456  119.656 1.00 23.58 ? 165  ALA C O     1 
ATOM   6658  C  CB    . ALA K  3 165 ? 34.486  41.143  121.639 1.00 23.49 ? 165  ALA C CB    1 
ATOM   6659  N  N     . THR K  3 166 ? 35.628  42.121  118.258 1.00 22.43 ? 166  THR C N     1 
ATOM   6660  C  CA    . THR K  3 166 ? 36.371  41.596  117.133 1.00 25.31 ? 166  THR C CA    1 
ATOM   6661  C  C     . THR K  3 166 ? 37.879  41.806  117.179 1.00 25.06 ? 166  THR C C     1 
ATOM   6662  O  O     . THR K  3 166 ? 38.616  41.226  116.379 1.00 27.39 ? 166  THR C O     1 
ATOM   6663  C  CB    . THR K  3 166 ? 35.805  42.176  115.808 1.00 27.81 ? 166  THR C CB    1 
ATOM   6664  O  OG1   . THR K  3 166 ? 36.146  43.562  115.704 1.00 26.89 ? 166  THR C OG1   1 
ATOM   6665  C  CG2   . THR K  3 166 ? 34.273  42.016  115.780 1.00 27.24 ? 166  THR C CG2   1 
ATOM   6666  N  N     . TYR K  3 167 ? 38.350  42.620  118.125 1.00 21.87 ? 167  TYR C N     1 
ATOM   6667  C  CA    . TYR K  3 167 ? 39.781  42.870  118.248 1.00 24.60 ? 167  TYR C CA    1 
ATOM   6668  C  C     . TYR K  3 167 ? 40.360  42.335  119.559 1.00 20.00 ? 167  TYR C C     1 
ATOM   6669  O  O     . TYR K  3 167 ? 41.543  42.533  119.821 1.00 22.52 ? 167  TYR C O     1 
ATOM   6670  C  CB    . TYR K  3 167 ? 40.080  44.362  118.144 1.00 21.37 ? 167  TYR C CB    1 
ATOM   6671  C  CG    . TYR K  3 167 ? 39.670  44.952  116.802 1.00 26.65 ? 167  TYR C CG    1 
ATOM   6672  C  CD1   . TYR K  3 167 ? 38.607  45.844  116.713 1.00 26.35 ? 167  TYR C CD1   1 
ATOM   6673  C  CD2   . TYR K  3 167 ? 40.325  44.582  115.623 1.00 28.63 ? 167  TYR C CD2   1 
ATOM   6674  C  CE1   . TYR K  3 167 ? 38.194  46.360  115.481 1.00 30.27 ? 167  TYR C CE1   1 
ATOM   6675  C  CE2   . TYR K  3 167 ? 39.912  45.094  114.372 1.00 32.40 ? 167  TYR C CE2   1 
ATOM   6676  C  CZ    . TYR K  3 167 ? 38.843  45.982  114.322 1.00 28.96 ? 167  TYR C CZ    1 
ATOM   6677  O  OH    . TYR K  3 167 ? 38.410  46.484  113.107 1.00 32.61 ? 167  TYR C OH    1 
ATOM   6678  N  N     . ALA K  3 168 ? 39.529  41.665  120.346 1.00 23.83 ? 168  ALA C N     1 
ATOM   6679  C  CA    . ALA K  3 168 ? 39.969  41.097  121.627 1.00 21.58 ? 168  ALA C CA    1 
ATOM   6680  C  C     . ALA K  3 168 ? 41.192  40.222  121.407 1.00 24.54 ? 168  ALA C C     1 
ATOM   6681  O  O     . ALA K  3 168 ? 41.182  39.329  120.569 1.00 23.58 ? 168  ALA C O     1 
ATOM   6682  C  CB    . ALA K  3 168 ? 38.862  40.286  122.240 1.00 22.25 ? 168  ALA C CB    1 
ATOM   6683  N  N     . SER K  3 169 ? 42.253  40.489  122.159 1.00 22.31 ? 169  SER C N     1 
ATOM   6684  C  CA    . SER K  3 169 ? 43.496  39.739  122.043 1.00 23.11 ? 169  SER C CA    1 
ATOM   6685  C  C     . SER K  3 169 ? 43.396  38.218  122.188 1.00 21.99 ? 169  SER C C     1 
ATOM   6686  O  O     . SER K  3 169 ? 44.111  37.479  121.498 1.00 23.03 ? 169  SER C O     1 
ATOM   6687  C  CB    . SER K  3 169 ? 44.490  40.270  123.071 1.00 26.41 ? 169  SER C CB    1 
ATOM   6688  O  OG    . SER K  3 169 ? 44.711  41.650  122.858 1.00 28.11 ? 169  SER C OG    1 
ATOM   6689  N  N     . LEU K  3 170 ? 42.532  37.759  123.078 1.00 21.61 ? 170  LEU C N     1 
ATOM   6690  C  CA    . LEU K  3 170 ? 42.373  36.328  123.326 1.00 22.83 ? 170  LEU C CA    1 
ATOM   6691  C  C     . LEU K  3 170 ? 41.685  35.507  122.241 1.00 26.53 ? 170  LEU C C     1 
ATOM   6692  O  O     . LEU K  3 170 ? 41.803  34.284  122.236 1.00 27.32 ? 170  LEU C O     1 
ATOM   6693  C  CB    . LEU K  3 170 ? 41.619  36.100  124.627 1.00 22.60 ? 170  LEU C CB    1 
ATOM   6694  C  CG    . LEU K  3 170 ? 42.455  36.291  125.884 1.00 23.06 ? 170  LEU C CG    1 
ATOM   6695  C  CD1   . LEU K  3 170 ? 41.531  36.372  127.098 1.00 23.43 ? 170  LEU C CD1   1 
ATOM   6696  C  CD2   . LEU K  3 170 ? 43.453  35.124  126.010 1.00 23.22 ? 170  LEU C CD2   1 
ATOM   6697  N  N     . ARG K  3 171 ? 40.998  36.171  121.317 1.00 27.77 ? 171  ARG C N     1 
ATOM   6698  C  CA    . ARG K  3 171 ? 40.269  35.448  120.277 1.00 29.06 ? 171  ARG C CA    1 
ATOM   6699  C  C     . ARG K  3 171 ? 41.131  34.856  119.182 1.00 26.59 ? 171  ARG C C     1 
ATOM   6700  O  O     . ARG K  3 171 ? 41.886  35.547  118.499 1.00 24.14 ? 171  ARG C O     1 
ATOM   6701  C  CB    . ARG K  3 171 ? 39.176  36.346  119.689 1.00 28.67 ? 171  ARG C CB    1 
ATOM   6702  C  CG    . ARG K  3 171 ? 38.158  36.732  120.750 1.00 28.94 ? 171  ARG C CG    1 
ATOM   6703  C  CD    . ARG K  3 171 ? 36.929  37.394  120.173 1.00 31.52 ? 171  ARG C CD    1 
ATOM   6704  N  NE    . ARG K  3 171 ? 36.136  36.486  119.335 1.00 30.37 ? 171  ARG C NE    1 
ATOM   6705  C  CZ    . ARG K  3 171 ? 34.985  36.827  118.757 1.00 33.86 ? 171  ARG C CZ    1 
ATOM   6706  N  NH1   . ARG K  3 171 ? 34.495  38.046  118.929 1.00 30.47 ? 171  ARG C NH1   1 
ATOM   6707  N  NH2   . ARG K  3 171 ? 34.329  35.953  117.998 1.00 32.08 ? 171  ARG C NH2   1 
ATOM   6708  N  N     . ALA K  3 172 ? 41.036  33.538  119.060 1.00 30.75 ? 172  ALA C N     1 
ATOM   6709  C  CA    . ALA K  3 172 ? 41.786  32.814  118.056 1.00 32.07 ? 172  ALA C CA    1 
ATOM   6710  C  C     . ALA K  3 172 ? 41.162  33.241  116.741 1.00 36.63 ? 172  ALA C C     1 
ATOM   6711  O  O     . ALA K  3 172 ? 39.949  33.354  116.623 1.00 39.46 ? 172  ALA C O     1 
ATOM   6712  C  CB    . ALA K  3 172 ? 41.631  31.313  118.257 1.00 34.17 ? 172  ALA C CB    1 
ATOM   6713  N  N     . GLY K  3 173 ? 41.992  33.493  115.756 1.00 36.21 ? 173  GLY C N     1 
ATOM   6714  C  CA    . GLY K  3 173 ? 41.440  33.920  114.491 1.00 42.76 ? 173  GLY C CA    1 
ATOM   6715  C  C     . GLY K  3 173 ? 42.570  34.371  113.619 1.00 42.46 ? 173  GLY C C     1 
ATOM   6716  O  O     . GLY K  3 173 ? 43.457  35.101  114.065 1.00 42.68 ? 173  GLY C O     1 
ATOM   6717  N  N     . ASN K  3 174 ? 42.529  33.924  112.372 1.00 44.20 ? 174  ASN C N     1 
ATOM   6718  C  CA    . ASN K  3 174 ? 43.548  34.247  111.402 1.00 44.05 ? 174  ASN C CA    1 
ATOM   6719  C  C     . ASN K  3 174 ? 44.077  35.655  111.607 1.00 44.21 ? 174  ASN C C     1 
ATOM   6720  O  O     . ASN K  3 174 ? 43.324  36.630  111.576 1.00 45.43 ? 174  ASN C O     1 
ATOM   6721  C  CB    . ASN K  3 174 ? 42.975  34.066  110.003 1.00 50.78 ? 174  ASN C CB    1 
ATOM   6722  C  CG    . ASN K  3 174 ? 42.338  32.701  109.827 1.00 56.59 ? 174  ASN C CG    1 
ATOM   6723  O  OD1   . ASN K  3 174 ? 42.918  31.678  110.207 1.00 60.03 ? 174  ASN C OD1   1 
ATOM   6724  N  ND2   . ASN K  3 174 ? 41.141  32.674  109.247 1.00 60.03 ? 174  ASN C ND2   1 
ATOM   6725  N  N     . GLY K  3 175 ? 45.385  35.732  111.839 1.00 40.82 ? 175  GLY C N     1 
ATOM   6726  C  CA    . GLY K  3 175 ? 46.040  37.001  112.077 1.00 41.99 ? 175  GLY C CA    1 
ATOM   6727  C  C     . GLY K  3 175 ? 46.505  37.153  113.522 1.00 40.80 ? 175  GLY C C     1 
ATOM   6728  O  O     . GLY K  3 175 ? 47.542  37.753  113.778 1.00 44.17 ? 175  GLY C O     1 
ATOM   6729  N  N     . ASN K  3 176 ? 45.747  36.595  114.464 1.00 39.22 ? 176  ASN C N     1 
ATOM   6730  C  CA    . ASN K  3 176 ? 46.072  36.699  115.894 1.00 36.93 ? 176  ASN C CA    1 
ATOM   6731  C  C     . ASN K  3 176 ? 47.141  35.723  116.389 1.00 31.97 ? 176  ASN C C     1 
ATOM   6732  O  O     . ASN K  3 176 ? 47.054  34.527  116.167 1.00 33.39 ? 176  ASN C O     1 
ATOM   6733  C  CB    . ASN K  3 176 ? 44.802  36.506  116.718 1.00 39.96 ? 176  ASN C CB    1 
ATOM   6734  C  CG    . ASN K  3 176 ? 43.945  37.755  116.775 1.00 49.51 ? 176  ASN C CG    1 
ATOM   6735  O  OD1   . ASN K  3 176 ? 43.600  38.342  115.740 1.00 50.08 ? 176  ASN C OD1   1 
ATOM   6736  N  ND2   . ASN K  3 176 ? 43.583  38.163  117.990 1.00 50.83 ? 176  ASN C ND2   1 
ATOM   6737  N  N     . MET K  3 177 ? 48.129  36.243  117.108 1.00 28.59 ? 177  MET C N     1 
ATOM   6738  C  CA    . MET K  3 177 ? 49.221  35.430  117.623 1.00 28.32 ? 177  MET C CA    1 
ATOM   6739  C  C     . MET K  3 177 ? 49.094  35.191  119.126 1.00 27.75 ? 177  MET C C     1 
ATOM   6740  O  O     . MET K  3 177 ? 48.351  35.887  119.819 1.00 25.74 ? 177  MET C O     1 
ATOM   6741  C  CB    . MET K  3 177 ? 50.552  36.127  117.353 1.00 31.20 ? 177  MET C CB    1 
ATOM   6742  C  CG    . MET K  3 177 ? 50.742  36.546  115.918 1.00 36.92 ? 177  MET C CG    1 
ATOM   6743  S  SD    . MET K  3 177 ? 52.090  37.731  115.749 1.00 47.15 ? 177  MET C SD    1 
ATOM   6744  C  CE    . MET K  3 177 ? 52.506  37.499  114.018 1.00 45.13 ? 177  MET C CE    1 
ATOM   6745  N  N     . PRO K  3 178 ? 49.816  34.187  119.637 1.00 27.20 ? 178  PRO C N     1 
ATOM   6746  C  CA    . PRO K  3 178 ? 49.801  33.850  121.065 1.00 24.58 ? 178  PRO C CA    1 
ATOM   6747  C  C     . PRO K  3 178 ? 50.281  35.051  121.868 1.00 22.25 ? 178  PRO C C     1 
ATOM   6748  O  O     . PRO K  3 178 ? 51.040  35.877  121.372 1.00 22.57 ? 178  PRO C O     1 
ATOM   6749  C  CB    . PRO K  3 178 ? 50.793  32.706  121.170 1.00 27.13 ? 178  PRO C CB    1 
ATOM   6750  C  CG    . PRO K  3 178 ? 50.740  32.074  119.817 1.00 31.32 ? 178  PRO C CG    1 
ATOM   6751  C  CD    . PRO K  3 178 ? 50.647  33.241  118.876 1.00 27.85 ? 178  PRO C CD    1 
ATOM   6752  N  N     . LEU K  3 179 ? 49.872  35.114  123.129 1.00 20.72 ? 179  LEU C N     1 
ATOM   6753  C  CA    . LEU K  3 179 ? 50.277  36.210  123.991 1.00 18.97 ? 179  LEU C CA    1 
ATOM   6754  C  C     . LEU K  3 179 ? 51.501  35.856  124.825 1.00 18.86 ? 179  LEU C C     1 
ATOM   6755  O  O     . LEU K  3 179 ? 51.633  34.722  125.285 1.00 18.62 ? 179  LEU C O     1 
ATOM   6756  C  CB    . LEU K  3 179 ? 49.140  36.561  124.937 1.00 19.85 ? 179  LEU C CB    1 
ATOM   6757  C  CG    . LEU K  3 179 ? 47.942  37.248  124.276 1.00 22.18 ? 179  LEU C CG    1 
ATOM   6758  C  CD1   . LEU K  3 179 ? 46.683  36.794  124.950 1.00 26.46 ? 179  LEU C CD1   1 
ATOM   6759  C  CD2   . LEU K  3 179 ? 48.125  38.757  124.371 1.00 26.66 ? 179  LEU C CD2   1 
ATOM   6760  N  N     . LEU K  3 180 ? 52.391  36.829  125.010 1.00 16.35 ? 180  LEU C N     1 
ATOM   6761  C  CA    . LEU K  3 180 ? 53.560  36.607  125.859 1.00 13.89 ? 180  LEU C CA    1 
ATOM   6762  C  C     . LEU K  3 180 ? 53.078  36.854  127.292 1.00 16.23 ? 180  LEU C C     1 
ATOM   6763  O  O     . LEU K  3 180 ? 52.624  37.958  127.620 1.00 16.74 ? 180  LEU C O     1 
ATOM   6764  C  CB    . LEU K  3 180 ? 54.683  37.595  125.533 1.00 17.26 ? 180  LEU C CB    1 
ATOM   6765  C  CG    . LEU K  3 180 ? 55.941  37.426  126.391 1.00 18.60 ? 180  LEU C CG    1 
ATOM   6766  C  CD1   . LEU K  3 180 ? 56.468  35.984  126.296 1.00 19.74 ? 180  LEU C CD1   1 
ATOM   6767  C  CD2   . LEU K  3 180 ? 56.981  38.422  125.921 1.00 19.53 ? 180  LEU C CD2   1 
ATOM   6768  N  N     . HIS K  3 181 ? 53.186  35.826  128.132 1.00 15.19 ? 181  HIS C N     1 
ATOM   6769  C  CA    . HIS K  3 181 ? 52.742  35.906  129.513 1.00 16.25 ? 181  HIS C CA    1 
ATOM   6770  C  C     . HIS K  3 181 ? 53.846  36.361  130.451 1.00 13.87 ? 181  HIS C C     1 
ATOM   6771  O  O     . HIS K  3 181 ? 53.613  37.172  131.355 1.00 14.40 ? 181  HIS C O     1 
ATOM   6772  C  CB    . HIS K  3 181 ? 52.215  34.542  129.976 1.00 14.31 ? 181  HIS C CB    1 
ATOM   6773  C  CG    . HIS K  3 181 ? 51.621  34.576  131.355 1.00 12.76 ? 181  HIS C CG    1 
ATOM   6774  N  ND1   . HIS K  3 181 ? 52.153  33.885  132.423 1.00 19.38 ? 181  HIS C ND1   1 
ATOM   6775  C  CD2   . HIS K  3 181 ? 50.544  35.245  131.830 1.00 11.57 ? 181  HIS C CD2   1 
ATOM   6776  C  CE1   . HIS K  3 181 ? 51.420  34.129  133.505 1.00 12.81 ? 181  HIS C CE1   1 
ATOM   6777  N  NE2   . HIS K  3 181 ? 50.442  34.950  133.168 1.00 21.19 ? 181  HIS C NE2   1 
ATOM   6778  N  N     . ALA K  3 182 ? 55.044  35.854  130.217 1.00 14.19 ? 182  ALA C N     1 
ATOM   6779  C  CA    . ALA K  3 182 ? 56.165  36.163  131.081 1.00 13.79 ? 182  ALA C CA    1 
ATOM   6780  C  C     . ALA K  3 182 ? 57.519  36.052  130.425 1.00 14.14 ? 182  ALA C C     1 
ATOM   6781  O  O     . ALA K  3 182 ? 57.740  35.187  129.573 1.00 13.65 ? 182  ALA C O     1 
ATOM   6782  C  CB    . ALA K  3 182 ? 56.128  35.210  132.303 1.00 14.63 ? 182  ALA C CB    1 
ATOM   6783  N  N     . SER K  3 183 ? 58.420  36.931  130.863 1.00 12.62 ? 183  SER C N     1 
ATOM   6784  C  CA    . SER K  3 183 ? 59.809  36.934  130.472 1.00 13.04 ? 183  SER C CA    1 
ATOM   6785  C  C     . SER K  3 183 ? 60.516  36.561  131.771 1.00 14.80 ? 183  SER C C     1 
ATOM   6786  O  O     . SER K  3 183 ? 60.387  37.265  132.782 1.00 15.47 ? 183  SER C O     1 
ATOM   6787  C  CB    . SER K  3 183 ? 60.262  38.333  130.054 1.00 16.82 ? 183  SER C CB    1 
ATOM   6788  O  OG    . SER K  3 183 ? 61.678  38.390  130.056 1.00 18.49 ? 183  SER C OG    1 
ATOM   6789  N  N     . ILE K  3 184 ? 61.225  35.442  131.749 1.00 13.67 ? 184  ILE C N     1 
ATOM   6790  C  CA    . ILE K  3 184 ? 61.945  34.957  132.926 1.00 13.19 ? 184  ILE C CA    1 
ATOM   6791  C  C     . ILE K  3 184 ? 63.433  34.948  132.590 1.00 15.85 ? 184  ILE C C     1 
ATOM   6792  O  O     . ILE K  3 184 ? 63.901  34.143  131.789 1.00 17.03 ? 184  ILE C O     1 
ATOM   6793  C  CB    . ILE K  3 184 ? 61.466  33.544  133.320 1.00 14.31 ? 184  ILE C CB    1 
ATOM   6794  C  CG1   . ILE K  3 184 ? 59.946  33.559  133.550 1.00 13.15 ? 184  ILE C CG1   1 
ATOM   6795  C  CG2   . ILE K  3 184 ? 62.228  33.054  134.608 1.00 17.56 ? 184  ILE C CG2   1 
ATOM   6796  C  CD1   . ILE K  3 184 ? 59.349  32.136  133.769 1.00 15.62 ? 184  ILE C CD1   1 
ATOM   6797  N  N     . SER K  3 185 ? 64.164  35.863  133.207 1.00 13.22 ? 185  SER C N     1 
ATOM   6798  C  CA    . SER K  3 185 ? 65.588  35.995  133.003 1.00 15.30 ? 185  SER C CA    1 
ATOM   6799  C  C     . SER K  3 185 ? 66.298  35.134  134.047 1.00 16.35 ? 185  SER C C     1 
ATOM   6800  O  O     . SER K  3 185 ? 65.920  35.157  135.215 1.00 15.73 ? 185  SER C O     1 
ATOM   6801  C  CB    . SER K  3 185 ? 65.959  37.475  133.170 1.00 19.07 ? 185  SER C CB    1 
ATOM   6802  O  OG    . SER K  3 185 ? 67.321  37.621  133.528 1.00 30.04 ? 185  SER C OG    1 
ATOM   6803  N  N     . CYS K  3 186 ? 67.280  34.346  133.618 1.00 12.13 ? 186  CYS C N     1 
ATOM   6804  C  CA    . CYS K  3 186 ? 68.041  33.519  134.551 1.00 12.36 ? 186  CYS C CA    1 
ATOM   6805  C  C     . CYS K  3 186 ? 69.487  33.975  134.665 1.00 13.37 ? 186  CYS C C     1 
ATOM   6806  O  O     . CYS K  3 186 ? 70.103  34.378  133.668 1.00 13.52 ? 186  CYS C O     1 
ATOM   6807  C  CB    . CYS K  3 186 ? 68.040  32.061  134.083 1.00 13.95 ? 186  CYS C CB    1 
ATOM   6808  S  SG    . CYS K  3 186 ? 66.390  31.318  134.036 1.00 15.84 ? 186  CYS C SG    1 
ATOM   6809  N  N     . LYS K  3 187 ? 70.031  33.931  135.879 1.00 12.76 ? 187  LYS C N     1 
ATOM   6810  C  CA    . LYS K  3 187 ? 71.431  34.270  136.130 1.00 13.05 ? 187  LYS C CA    1 
ATOM   6811  C  C     . LYS K  3 187 ? 71.945  33.286  137.170 1.00 15.20 ? 187  LYS C C     1 
ATOM   6812  O  O     . LYS K  3 187 ? 71.596  33.378  138.344 1.00 15.23 ? 187  LYS C O     1 
ATOM   6813  C  CB    . LYS K  3 187 ? 71.585  35.711  136.636 1.00 14.58 ? 187  LYS C CB    1 
ATOM   6814  C  CG    . LYS K  3 187 ? 71.106  36.721  135.543 1.00 12.81 ? 187  LYS C CG    1 
ATOM   6815  C  CD    . LYS K  3 187 ? 71.470  38.182  135.899 1.00 15.65 ? 187  LYS C CD    1 
ATOM   6816  C  CE    . LYS K  3 187 ? 70.996  39.154  134.790 1.00 17.67 ? 187  LYS C CE    1 
ATOM   6817  N  NZ    . LYS K  3 187 ? 71.609  38.761  133.504 1.00 19.13 ? 187  LYS C NZ    1 
ATOM   6818  N  N     . TRP K  3 188 ? 72.792  32.366  136.728 1.00 14.03 ? 188  TRP C N     1 
ATOM   6819  C  CA    . TRP K  3 188 ? 73.364  31.359  137.636 1.00 13.33 ? 188  TRP C CA    1 
ATOM   6820  C  C     . TRP K  3 188 ? 74.123  32.108  138.746 1.00 16.15 ? 188  TRP C C     1 
ATOM   6821  O  O     . TRP K  3 188 ? 73.989  31.796  139.948 1.00 15.57 ? 188  TRP C O     1 
ATOM   6822  C  CB    . TRP K  3 188 ? 74.266  30.421  136.824 1.00 13.58 ? 188  TRP C CB    1 
ATOM   6823  C  CG    . TRP K  3 188 ? 75.035  29.438  137.662 1.00 14.86 ? 188  TRP C CG    1 
ATOM   6824  C  CD1   . TRP K  3 188 ? 76.393  29.351  137.759 1.00 14.80 ? 188  TRP C CD1   1 
ATOM   6825  C  CD2   . TRP K  3 188 ? 74.499  28.446  138.551 1.00 15.96 ? 188  TRP C CD2   1 
ATOM   6826  N  NE1   . TRP K  3 188 ? 76.751  28.367  138.662 1.00 17.45 ? 188  TRP C NE1   1 
ATOM   6827  C  CE2   . TRP K  3 188 ? 75.608  27.795  139.163 1.00 15.13 ? 188  TRP C CE2   1 
ATOM   6828  C  CE3   . TRP K  3 188 ? 73.198  28.046  138.894 1.00 15.64 ? 188  TRP C CE3   1 
ATOM   6829  C  CZ2   . TRP K  3 188 ? 75.448  26.760  140.109 1.00 17.66 ? 188  TRP C CZ2   1 
ATOM   6830  C  CZ3   . TRP K  3 188 ? 73.039  27.025  139.827 1.00 18.15 ? 188  TRP C CZ3   1 
ATOM   6831  C  CH2   . TRP K  3 188 ? 74.165  26.394  140.424 1.00 17.97 ? 188  TRP C CH2   1 
ATOM   6832  N  N     . THR K  3 189 ? 74.948  33.076  138.356 1.00 12.63 ? 189  THR C N     1 
ATOM   6833  C  CA    . THR K  3 189 ? 75.645  33.924  139.313 1.00 12.88 ? 189  THR C CA    1 
ATOM   6834  C  C     . THR K  3 189 ? 75.536  35.338  138.773 1.00 12.46 ? 189  THR C C     1 
ATOM   6835  O  O     . THR K  3 189 ? 75.151  35.541  137.617 1.00 14.53 ? 189  THR C O     1 
ATOM   6836  C  CB    . THR K  3 189 ? 77.141  33.594  139.455 1.00 14.31 ? 189  THR C CB    1 
ATOM   6837  O  OG1   . THR K  3 189 ? 77.801  33.788  138.195 1.00 14.51 ? 189  THR C OG1   1 
ATOM   6838  C  CG2   . THR K  3 189 ? 77.319  32.138  139.876 1.00 13.58 ? 189  THR C CG2   1 
ATOM   6839  N  N     . ILE K  3 190 ? 75.900  36.294  139.611 1.00 13.84 ? 190  ILE C N     1 
ATOM   6840  C  CA    . ILE K  3 190 ? 75.838  37.699  139.229 1.00 14.57 ? 190  ILE C CA    1 
ATOM   6841  C  C     . ILE K  3 190 ? 77.142  38.476  139.423 1.00 17.78 ? 190  ILE C C     1 
ATOM   6842  O  O     . ILE K  3 190 ? 77.944  38.149  140.285 1.00 14.85 ? 190  ILE C O     1 
ATOM   6843  C  CB    . ILE K  3 190 ? 74.741  38.408  140.096 1.00 14.30 ? 190  ILE C CB    1 
ATOM   6844  C  CG1   . ILE K  3 190 ? 73.346  37.919  139.673 1.00 12.50 ? 190  ILE C CG1   1 
ATOM   6845  C  CG2   . ILE K  3 190 ? 74.870  39.943  139.994 1.00 16.46 ? 190  ILE C CG2   1 
ATOM   6846  C  CD1   . ILE K  3 190 ? 72.225  38.346  140.632 1.00 17.20 ? 190  ILE C CD1   1 
ATOM   6847  N  N     . ARG K  3 191 ? 77.387  39.443  138.537 1.00 14.85 ? 191  ARG C N     1 
ATOM   6848  C  CA    . ARG K  3 191 ? 78.421  40.453  138.778 1.00 15.62 ? 191  ARG C CA    1 
ATOM   6849  C  C     . ARG K  3 191 ? 77.548  41.692  138.521 1.00 14.61 ? 191  ARG C C     1 
ATOM   6850  O  O     . ARG K  3 191 ? 76.686  41.684  137.626 1.00 14.34 ? 191  ARG C O     1 
ATOM   6851  C  CB    . ARG K  3 191 ? 79.598  40.413  137.817 1.00 17.68 ? 191  ARG C CB    1 
ATOM   6852  C  CG    . ARG K  3 191 ? 80.504  39.206  138.025 1.00 14.12 ? 191  ARG C CG    1 
ATOM   6853  C  CD    . ARG K  3 191 ? 81.146  39.193  139.416 1.00 16.33 ? 191  ARG C CD    1 
ATOM   6854  N  NE    . ARG K  3 191 ? 82.098  38.077  139.518 1.00 16.00 ? 191  ARG C NE    1 
ATOM   6855  C  CZ    . ARG K  3 191 ? 81.808  36.842  139.939 1.00 16.59 ? 191  ARG C CZ    1 
ATOM   6856  N  NH1   . ARG K  3 191 ? 80.582  36.532  140.320 1.00 15.16 ? 191  ARG C NH1   1 
ATOM   6857  N  NH2   . ARG K  3 191 ? 82.762  35.901  139.948 1.00 15.41 ? 191  ARG C NH2   1 
ATOM   6858  N  N     . SER K  3 192 ? 77.772  42.743  139.294 1.00 13.93 ? 192  SER C N     1 
ATOM   6859  C  CA    . SER K  3 192 ? 76.953  43.947  139.203 1.00 14.12 ? 192  SER C CA    1 
ATOM   6860  C  C     . SER K  3 192 ? 76.924  44.656  137.865 1.00 13.44 ? 192  SER C C     1 
ATOM   6861  O  O     . SER K  3 192 ? 75.960  45.370  137.574 1.00 15.74 ? 192  SER C O     1 
ATOM   6862  C  CB    . SER K  3 192 ? 77.318  44.937  140.316 1.00 16.57 ? 192  SER C CB    1 
ATOM   6863  O  OG    . SER K  3 192 ? 78.647  45.431  140.198 1.00 17.32 ? 192  SER C OG    1 
ATOM   6864  N  N     . ASP K  3 193 ? 77.945  44.461  137.045 1.00 12.99 ? 193  ASP C N     1 
ATOM   6865  C  CA    . ASP K  3 193 ? 77.926  45.108  135.752 1.00 15.20 ? 193  ASP C CA    1 
ATOM   6866  C  C     . ASP K  3 193 ? 77.041  44.309  134.787 1.00 13.98 ? 193  ASP C C     1 
ATOM   6867  O  O     . ASP K  3 193 ? 76.116  44.869  134.173 1.00 15.57 ? 193  ASP C O     1 
ATOM   6868  C  CB    . ASP K  3 193 ? 79.357  45.261  135.152 1.00 14.42 ? 193  ASP C CB    1 
ATOM   6869  C  CG    . ASP K  3 193 ? 80.133  43.929  135.034 1.00 18.14 ? 193  ASP C CG    1 
ATOM   6870  O  OD1   . ASP K  3 193 ? 80.873  43.742  134.035 1.00 14.49 ? 193  ASP C OD1   1 
ATOM   6871  O  OD2   . ASP K  3 193 ? 80.038  43.071  135.939 1.00 15.65 ? 193  ASP C OD2   1 
ATOM   6872  N  N     . ARG K  3 194 ? 77.309  43.007  134.644 1.00 13.91 ? 194  ARG C N     1 
ATOM   6873  C  CA    . ARG K  3 194 ? 76.548  42.191  133.719 1.00 14.06 ? 194  ARG C CA    1 
ATOM   6874  C  C     . ARG K  3 194 ? 75.121  41.924  134.134 1.00 15.46 ? 194  ARG C C     1 
ATOM   6875  O  O     . ARG K  3 194 ? 74.302  41.513  133.323 1.00 21.08 ? 194  ARG C O     1 
ATOM   6876  C  CB    . ARG K  3 194 ? 77.296  40.883  133.395 1.00 15.54 ? 194  ARG C CB    1 
ATOM   6877  C  CG    . ARG K  3 194 ? 77.660  39.948  134.586 1.00 14.70 ? 194  ARG C CG    1 
ATOM   6878  C  CD    . ARG K  3 194 ? 78.462  38.677  134.073 1.00 15.02 ? 194  ARG C CD    1 
ATOM   6879  N  NE    . ARG K  3 194 ? 78.987  37.827  135.157 1.00 17.80 ? 194  ARG C NE    1 
ATOM   6880  C  CZ    . ARG K  3 194 ? 78.255  37.028  135.920 1.00 20.05 ? 194  ARG C CZ    1 
ATOM   6881  N  NH1   . ARG K  3 194 ? 76.942  36.938  135.729 1.00 19.52 ? 194  ARG C NH1   1 
ATOM   6882  N  NH2   . ARG K  3 194 ? 78.829  36.338  136.910 1.00 20.39 ? 194  ARG C NH2   1 
ATOM   6883  N  N     . ALA K  3 195 ? 74.784  42.183  135.392 1.00 12.61 ? 195  ALA C N     1 
ATOM   6884  C  CA    . ALA K  3 195 ? 73.395  41.957  135.807 1.00 14.06 ? 195  ALA C CA    1 
ATOM   6885  C  C     . ALA K  3 195 ? 72.442  42.978  135.190 1.00 11.12 ? 195  ALA C C     1 
ATOM   6886  O  O     . ALA K  3 195 ? 71.247  42.741  135.113 1.00 11.95 ? 195  ALA C O     1 
ATOM   6887  C  CB    . ALA K  3 195 ? 73.296  42.052  137.318 1.00 20.33 ? 195  ALA C CB    1 
ATOM   6888  N  N     . GLN K  3 196 ? 72.974  44.128  134.785 1.00 11.69 ? 196  GLN C N     1 
ATOM   6889  C  CA    . GLN K  3 196 ? 72.134  45.200  134.254 1.00 14.16 ? 196  GLN C CA    1 
ATOM   6890  C  C     . GLN K  3 196 ? 71.463  44.922  132.915 1.00 12.02 ? 196  GLN C C     1 
ATOM   6891  O  O     . GLN K  3 196 ? 70.540  45.661  132.520 1.00 12.85 ? 196  GLN C O     1 
ATOM   6892  C  CB    . GLN K  3 196 ? 72.937  46.504  134.188 1.00 13.67 ? 196  GLN C CB    1 
ATOM   6893  C  CG    . GLN K  3 196 ? 73.627  46.860  135.513 1.00 13.80 ? 196  GLN C CG    1 
ATOM   6894  C  CD    . GLN K  3 196 ? 72.680  46.786  136.711 1.00 18.05 ? 196  GLN C CD    1 
ATOM   6895  O  OE1   . GLN K  3 196 ? 71.559  47.255  136.632 1.00 16.96 ? 196  GLN C OE1   1 
ATOM   6896  N  NE2   . GLN K  3 196 ? 73.142  46.189  137.832 1.00 14.54 ? 196  GLN C NE2   1 
ATOM   6897  N  N     . ASN K  3 197 ? 71.887  43.886  132.195 1.00 12.11 ? 197  ASN C N     1 
ATOM   6898  C  CA    . ASN K  3 197 ? 71.162  43.609  130.964 1.00 13.60 ? 197  ASN C CA    1 
ATOM   6899  C  C     . ASN K  3 197 ? 69.709  43.165  131.280 1.00 14.13 ? 197  ASN C C     1 
ATOM   6900  O  O     . ASN K  3 197 ? 68.837  43.208  130.410 1.00 14.57 ? 197  ASN C O     1 
ATOM   6901  C  CB    . ASN K  3 197 ? 71.911  42.590  130.067 1.00 13.47 ? 197  ASN C CB    1 
ATOM   6902  C  CG    . ASN K  3 197 ? 71.958  41.183  130.640 1.00 14.99 ? 197  ASN C CG    1 
ATOM   6903  O  OD1   . ASN K  3 197 ? 71.721  40.971  131.823 1.00 15.24 ? 197  ASN C OD1   1 
ATOM   6904  N  ND2   . ASN K  3 197 ? 72.286  40.209  129.784 1.00 15.14 ? 197  ASN C ND2   1 
ATOM   6905  N  N     . ALA K  3 198 ? 69.416  42.768  132.525 1.00 13.62 ? 198  ALA C N     1 
ATOM   6906  C  CA    . ALA K  3 198 ? 68.034  42.401  132.858 1.00 14.02 ? 198  ALA C CA    1 
ATOM   6907  C  C     . ALA K  3 198 ? 67.173  43.676  132.877 1.00 13.72 ? 198  ALA C C     1 
ATOM   6908  O  O     . ALA K  3 198 ? 65.981  43.644  132.554 1.00 15.14 ? 198  ALA C O     1 
ATOM   6909  C  CB    . ALA K  3 198 ? 67.991  41.711  134.255 1.00 13.97 ? 198  ALA C CB    1 
ATOM   6910  N  N     . ARG K  3 199 ? 67.775  44.791  133.312 1.00 12.93 ? 199  ARG C N     1 
ATOM   6911  C  CA    . ARG K  3 199 ? 67.052  46.053  133.349 1.00 14.25 ? 199  ARG C CA    1 
ATOM   6912  C  C     . ARG K  3 199 ? 66.820  46.591  131.949 1.00 14.64 ? 199  ARG C C     1 
ATOM   6913  O  O     . ARG K  3 199 ? 65.737  47.084  131.666 1.00 14.72 ? 199  ARG C O     1 
ATOM   6914  C  CB    . ARG K  3 199 ? 67.798  47.104  134.185 1.00 16.50 ? 199  ARG C CB    1 
ATOM   6915  C  CG    . ARG K  3 199 ? 67.841  46.759  135.690 1.00 16.37 ? 199  ARG C CG    1 
ATOM   6916  C  CD    . ARG K  3 199 ? 68.485  47.907  136.516 1.00 16.70 ? 199  ARG C CD    1 
ATOM   6917  N  NE    . ARG K  3 199 ? 68.949  47.498  137.860 1.00 20.77 ? 199  ARG C NE    1 
ATOM   6918  C  CZ    . ARG K  3 199 ? 68.210  47.525  138.959 1.00 23.05 ? 199  ARG C CZ    1 
ATOM   6919  N  NH1   . ARG K  3 199 ? 66.955  47.945  138.902 1.00 24.43 ? 199  ARG C NH1   1 
ATOM   6920  N  NH2   . ARG K  3 199 ? 68.722  47.137  140.118 1.00 24.16 ? 199  ARG C NH2   1 
ATOM   6921  N  N     . SER K  3 200 ? 67.816  46.468  131.062 1.00 15.03 ? 200  SER C N     1 
ATOM   6922  C  CA    . SER K  3 200 ? 67.626  46.994  129.708 1.00 16.39 ? 200  SER C CA    1 
ATOM   6923  C  C     . SER K  3 200 ? 66.613  46.136  128.948 1.00 17.76 ? 200  SER C C     1 
ATOM   6924  O  O     . SER K  3 200 ? 65.772  46.670  128.208 1.00 14.90 ? 200  SER C O     1 
ATOM   6925  C  CB    . SER K  3 200 ? 68.969  47.100  128.947 1.00 17.77 ? 200  SER C CB    1 
ATOM   6926  O  OG    . SER K  3 200 ? 69.628  45.865  128.856 1.00 19.02 ? 200  SER C OG    1 
ATOM   6927  N  N     . GLU K  3 201 ? 66.660  44.820  129.146 1.00 14.86 ? 201  GLU C N     1 
ATOM   6928  C  CA    . GLU K  3 201 ? 65.677  43.946  128.476 1.00 16.94 ? 201  GLU C CA    1 
ATOM   6929  C  C     . GLU K  3 201 ? 64.270  44.246  129.004 1.00 15.30 ? 201  GLU C C     1 
ATOM   6930  O  O     . GLU K  3 201 ? 63.304  44.306  128.235 1.00 16.27 ? 201  GLU C O     1 
ATOM   6931  C  CB    . GLU K  3 201 ? 66.079  42.465  128.645 1.00 19.43 ? 201  GLU C CB    1 
ATOM   6932  C  CG    . GLU K  3 201 ? 67.262  42.154  127.693 1.00 28.68 ? 201  GLU C CG    1 
ATOM   6933  C  CD    . GLU K  3 201 ? 67.792  40.727  127.711 1.00 31.71 ? 201  GLU C CD    1 
ATOM   6934  O  OE1   . GLU K  3 201 ? 66.981  39.760  127.773 1.00 25.76 ? 201  GLU C OE1   1 
ATOM   6935  O  OE2   . GLU K  3 201 ? 69.043  40.590  127.633 1.00 33.79 ? 201  GLU C OE2   1 
ATOM   6936  N  N     . GLY K  3 202 ? 64.169  44.474  130.316 1.00 14.06 ? 202  GLY C N     1 
ATOM   6937  C  CA    . GLY K  3 202 ? 62.885  44.811  130.916 1.00 15.02 ? 202  GLY C CA    1 
ATOM   6938  C  C     . GLY K  3 202 ? 62.358  46.135  130.355 1.00 16.00 ? 202  GLY C C     1 
ATOM   6939  O  O     . GLY K  3 202 ? 61.169  46.249  130.043 1.00 16.17 ? 202  GLY C O     1 
ATOM   6940  N  N     . LEU K  3 203 ? 63.231  47.129  130.226 1.00 14.18 ? 203  LEU C N     1 
ATOM   6941  C  CA    . LEU K  3 203 ? 62.792  48.427  129.688 1.00 15.64 ? 203  LEU C CA    1 
ATOM   6942  C  C     . LEU K  3 203 ? 62.323  48.288  128.232 1.00 16.16 ? 203  LEU C C     1 
ATOM   6943  O  O     . LEU K  3 203 ? 61.354  48.948  127.815 1.00 15.83 ? 203  LEU C O     1 
ATOM   6944  C  CB    . LEU K  3 203 ? 63.927  49.438  129.773 1.00 19.28 ? 203  LEU C CB    1 
ATOM   6945  C  CG    . LEU K  3 203 ? 63.543  50.914  129.694 1.00 29.24 ? 203  LEU C CG    1 
ATOM   6946  C  CD1   . LEU K  3 203 ? 62.562  51.262  130.828 1.00 33.43 ? 203  LEU C CD1   1 
ATOM   6947  C  CD2   . LEU K  3 203 ? 64.819  51.742  129.827 1.00 33.99 ? 203  LEU C CD2   1 
ATOM   6948  N  N     . ASN K  3 204 ? 62.977  47.441  127.455 1.00 16.26 ? 204  ASN C N     1 
ATOM   6949  C  CA    . ASN K  3 204 ? 62.517  47.262  126.068 1.00 16.99 ? 204  ASN C CA    1 
ATOM   6950  C  C     . ASN K  3 204 ? 61.121  46.643  126.032 1.00 18.76 ? 204  ASN C C     1 
ATOM   6951  O  O     . ASN K  3 204 ? 60.290  46.999  125.187 1.00 19.01 ? 204  ASN C O     1 
ATOM   6952  C  CB    . ASN K  3 204 ? 63.488  46.389  125.288 1.00 21.89 ? 204  ASN C CB    1 
ATOM   6953  C  CG    . ASN K  3 204 ? 64.725  47.153  124.876 1.00 32.78 ? 204  ASN C CG    1 
ATOM   6954  O  OD1   . ASN K  3 204 ? 64.679  48.373  124.672 1.00 37.43 ? 204  ASN C OD1   1 
ATOM   6955  N  ND2   . ASN K  3 204 ? 65.827  46.450  124.739 1.00 32.32 ? 204  ASN C ND2   1 
ATOM   6956  N  N     . LEU K  3 205 ? 60.848  45.701  126.933 1.00 13.89 ? 205  LEU C N     1 
ATOM   6957  C  CA    . LEU K  3 205 ? 59.530  45.095  126.975 1.00 13.14 ? 205  LEU C CA    1 
ATOM   6958  C  C     . LEU K  3 205 ? 58.490  46.152  127.370 1.00 14.47 ? 205  LEU C C     1 
ATOM   6959  O  O     . LEU K  3 205 ? 57.361  46.146  126.873 1.00 14.40 ? 205  LEU C O     1 
ATOM   6960  C  CB    . LEU K  3 205 ? 59.504  43.937  127.994 1.00 13.81 ? 205  LEU C CB    1 
ATOM   6961  C  CG    . LEU K  3 205 ? 60.344  42.727  127.580 1.00 17.10 ? 205  LEU C CG    1 
ATOM   6962  C  CD1   . LEU K  3 205 ? 60.363  41.719  128.750 1.00 21.66 ? 205  LEU C CD1   1 
ATOM   6963  C  CD2   . LEU K  3 205 ? 59.770  42.066  126.337 1.00 20.79 ? 205  LEU C CD2   1 
ATOM   6964  N  N     . VAL K  3 206 ? 58.857  47.056  128.281 1.00 12.90 ? 206  VAL C N     1 
ATOM   6965  C  CA    . VAL K  3 206 ? 57.938  48.101  128.718 1.00 12.79 ? 206  VAL C CA    1 
ATOM   6966  C  C     . VAL K  3 206 ? 57.646  49.099  127.592 1.00 14.89 ? 206  VAL C C     1 
ATOM   6967  O  O     . VAL K  3 206 ? 56.484  49.369  127.260 1.00 16.10 ? 206  VAL C O     1 
ATOM   6968  C  CB    . VAL K  3 206 ? 58.543  48.920  129.916 1.00 15.17 ? 206  VAL C CB    1 
ATOM   6969  C  CG1   . VAL K  3 206 ? 57.716  50.197  130.162 1.00 17.57 ? 206  VAL C CG1   1 
ATOM   6970  C  CG2   . VAL K  3 206 ? 58.580  48.060  131.185 1.00 16.76 ? 206  VAL C CG2   1 
ATOM   6971  N  N     . ARG K  3 207 ? 58.717  49.611  127.002 1.00 16.00 ? 207  ARG C N     1 
ATOM   6972  C  CA    . ARG K  3 207 ? 58.605  50.654  125.993 1.00 16.38 ? 207  ARG C CA    1 
ATOM   6973  C  C     . ARG K  3 207 ? 57.957  50.272  124.671 1.00 19.50 ? 207  ARG C C     1 
ATOM   6974  O  O     . ARG K  3 207 ? 57.351  51.125  123.996 1.00 20.21 ? 207  ARG C O     1 
ATOM   6975  C  CB    . ARG K  3 207 ? 60.002  51.241  125.714 1.00 20.82 ? 207  ARG C CB    1 
ATOM   6976  C  CG    . ARG K  3 207 ? 60.592  51.951  126.921 1.00 27.78 ? 207  ARG C CG    1 
ATOM   6977  C  CD    . ARG K  3 207 ? 62.008  52.448  126.676 1.00 42.21 ? 207  ARG C CD    1 
ATOM   6978  N  NE    . ARG K  3 207 ? 62.472  53.247  127.806 1.00 47.31 ? 207  ARG C NE    1 
ATOM   6979  C  CZ    . ARG K  3 207 ? 63.719  53.683  127.964 1.00 53.32 ? 207  ARG C CZ    1 
ATOM   6980  N  NH1   . ARG K  3 207 ? 64.651  53.399  127.059 1.00 51.41 ? 207  ARG C NH1   1 
ATOM   6981  N  NH2   . ARG K  3 207 ? 64.034  54.398  129.043 1.00 53.56 ? 207  ARG C NH2   1 
ATOM   6982  N  N     . ASN K  3 208 ? 58.058  49.008  124.304 1.00 17.09 ? 208  ASN C N     1 
ATOM   6983  C  CA    . ASN K  3 208 ? 57.532  48.581  122.999 1.00 18.11 ? 208  ASN C CA    1 
ATOM   6984  C  C     . ASN K  3 208 ? 56.249  47.779  122.970 1.00 20.01 ? 208  ASN C C     1 
ATOM   6985  O  O     . ASN K  3 208 ? 55.796  47.348  121.901 1.00 22.34 ? 208  ASN C O     1 
ATOM   6986  C  CB    . ASN K  3 208 ? 58.625  47.795  122.277 1.00 20.53 ? 208  ASN C CB    1 
ATOM   6987  C  CG    . ASN K  3 208 ? 59.812  48.670  121.908 1.00 27.90 ? 208  ASN C CG    1 
ATOM   6988  O  OD1   . ASN K  3 208 ? 59.664  49.622  121.140 1.00 31.31 ? 208  ASN C OD1   1 
ATOM   6989  N  ND2   . ASN K  3 208 ? 60.984  48.374  122.466 1.00 24.62 ? 208  ASN C ND2   1 
ATOM   6990  N  N     . ARG K  3 209 ? 55.625  47.574  124.121 1.00 17.70 ? 209  ARG C N     1 
ATOM   6991  C  CA    . ARG K  3 209 ? 54.439  46.756  124.158 1.00 15.59 ? 209  ARG C CA    1 
ATOM   6992  C  C     . ARG K  3 209 ? 53.146  47.359  123.602 1.00 18.18 ? 209  ARG C C     1 
ATOM   6993  O  O     . ARG K  3 209 ? 52.940  48.570  123.617 1.00 20.54 ? 209  ARG C O     1 
ATOM   6994  C  CB    . ARG K  3 209 ? 54.134  46.347  125.599 1.00 17.68 ? 209  ARG C CB    1 
ATOM   6995  C  CG    . ARG K  3 209 ? 53.444  47.483  126.374 1.00 20.52 ? 209  ARG C CG    1 
ATOM   6996  C  CD    . ARG K  3 209 ? 53.285  47.181  127.867 1.00 16.30 ? 209  ARG C CD    1 
ATOM   6997  N  NE    . ARG K  3 209 ? 52.422  48.168  128.521 1.00 15.04 ? 209  ARG C NE    1 
ATOM   6998  C  CZ    . ARG K  3 209 ? 52.814  49.356  129.001 1.00 14.98 ? 209  ARG C CZ    1 
ATOM   6999  N  NH1   . ARG K  3 209 ? 54.085  49.746  128.925 1.00 14.65 ? 209  ARG C NH1   1 
ATOM   7000  N  NH2   . ARG K  3 209 ? 51.914  50.177  129.545 1.00 15.37 ? 209  ARG C NH2   1 
ATOM   7001  N  N     . LYS K  3 210 ? 52.303  46.460  123.115 1.00 19.22 ? 210  LYS C N     1 
ATOM   7002  C  CA    . LYS K  3 210 ? 50.951  46.791  122.691 1.00 19.88 ? 210  LYS C CA    1 
ATOM   7003  C  C     . LYS K  3 210 ? 50.165  45.733  123.458 1.00 23.84 ? 210  LYS C C     1 
ATOM   7004  O  O     . LYS K  3 210 ? 50.197  44.555  123.113 1.00 29.43 ? 210  LYS C O     1 
ATOM   7005  C  CB    . LYS K  3 210 ? 50.804  46.638  121.182 1.00 22.40 ? 210  LYS C CB    1 
ATOM   7006  C  CG    . LYS K  3 210 ? 51.571  47.701  120.427 1.00 19.68 ? 210  LYS C CG    1 
ATOM   7007  C  CD    . LYS K  3 210 ? 51.256  47.656  118.940 1.00 25.50 ? 210  LYS C CD    1 
ATOM   7008  C  CE    . LYS K  3 210 ? 52.138  48.628  118.184 1.00 25.32 ? 210  LYS C CE    1 
ATOM   7009  N  NZ    . LYS K  3 210 ? 51.781  48.625  116.729 1.00 28.81 ? 210  LYS C NZ    1 
ATOM   7010  N  N     . GLY K  3 211 ? 49.486  46.141  124.523 1.00 22.91 ? 211  GLY C N     1 
ATOM   7011  C  CA    . GLY K  3 211 ? 48.750  45.188  125.340 1.00 21.85 ? 211  GLY C CA    1 
ATOM   7012  C  C     . GLY K  3 211 ? 49.334  45.210  126.747 1.00 18.33 ? 211  GLY C C     1 
ATOM   7013  O  O     . GLY K  3 211 ? 50.195  46.041  127.030 1.00 18.12 ? 211  GLY C O     1 
ATOM   7014  N  N     . ARG K  3 212 ? 48.878  44.316  127.617 1.00 18.61 ? 212  ARG C N     1 
ATOM   7015  C  CA    . ARG K  3 212 ? 49.383  44.275  128.993 1.00 17.40 ? 212  ARG C CA    1 
ATOM   7016  C  C     . ARG K  3 212 ? 50.821  43.781  129.021 1.00 16.28 ? 212  ARG C C     1 
ATOM   7017  O  O     . ARG K  3 212 ? 51.179  42.829  128.328 1.00 19.29 ? 212  ARG C O     1 
ATOM   7018  C  CB    . ARG K  3 212 ? 48.517  43.356  129.882 1.00 16.94 ? 212  ARG C CB    1 
ATOM   7019  C  CG    . ARG K  3 212 ? 48.950  43.449  131.382 1.00 16.42 ? 212  ARG C CG    1 
ATOM   7020  C  CD    . ARG K  3 212 ? 48.125  42.570  132.342 1.00 18.18 ? 212  ARG C CD    1 
ATOM   7021  N  NE    . ARG K  3 212 ? 48.567  42.789  133.725 1.00 20.61 ? 212  ARG C NE    1 
ATOM   7022  C  CZ    . ARG K  3 212 ? 48.095  42.156  134.800 1.00 18.82 ? 212  ARG C CZ    1 
ATOM   7023  N  NH1   . ARG K  3 212 ? 47.147  41.235  134.689 1.00 19.67 ? 212  ARG C NH1   1 
ATOM   7024  N  NH2   . ARG K  3 212 ? 48.572  42.463  136.006 1.00 21.68 ? 212  ARG C NH2   1 
ATOM   7025  N  N     . LEU K  3 213 ? 51.632  44.421  129.854 1.00 13.92 ? 213  LEU C N     1 
ATOM   7026  C  CA    . LEU K  3 213 ? 53.026  44.060  129.996 1.00 14.67 ? 213  LEU C CA    1 
ATOM   7027  C  C     . LEU K  3 213 ? 53.112  42.632  130.553 1.00 15.76 ? 213  LEU C C     1 
ATOM   7028  O  O     . LEU K  3 213 ? 52.337  42.286  131.452 1.00 15.01 ? 213  LEU C O     1 
ATOM   7029  C  CB    . LEU K  3 213 ? 53.701  45.016  130.998 1.00 14.61 ? 213  LEU C CB    1 
ATOM   7030  C  CG    . LEU K  3 213 ? 55.227  44.870  131.154 1.00 14.14 ? 213  LEU C CG    1 
ATOM   7031  C  CD1   . LEU K  3 213 ? 55.913  45.330  129.851 1.00 17.61 ? 213  LEU C CD1   1 
ATOM   7032  C  CD2   . LEU K  3 213 ? 55.754  45.753  132.322 1.00 13.85 ? 213  LEU C CD2   1 
ATOM   7033  N  N     . PRO K  3 214 ? 54.042  41.806  130.036 1.00 13.77 ? 214  PRO C N     1 
ATOM   7034  C  CA    . PRO K  3 214 ? 54.161  40.436  130.571 1.00 13.25 ? 214  PRO C CA    1 
ATOM   7035  C  C     . PRO K  3 214 ? 54.782  40.541  131.970 1.00 13.35 ? 214  PRO C C     1 
ATOM   7036  O  O     . PRO K  3 214 ? 55.298  41.588  132.345 1.00 13.69 ? 214  PRO C O     1 
ATOM   7037  C  CB    . PRO K  3 214 ? 55.208  39.768  129.669 1.00 19.95 ? 214  PRO C CB    1 
ATOM   7038  C  CG    . PRO K  3 214 ? 55.235  40.626  128.418 1.00 24.09 ? 214  PRO C CG    1 
ATOM   7039  C  CD    . PRO K  3 214 ? 54.947  42.027  128.888 1.00 15.59 ? 214  PRO C CD    1 
ATOM   7040  N  N     . HIS K  3 215 ? 54.727  39.448  132.717 1.00 15.56 ? 215  HIS C N     1 
ATOM   7041  C  CA    . HIS K  3 215 ? 55.481  39.393  133.969 1.00 16.40 ? 215  HIS C CA    1 
ATOM   7042  C  C     . HIS K  3 215 ? 56.960  39.560  133.507 1.00 13.88 ? 215  HIS C C     1 
ATOM   7043  O  O     . HIS K  3 215 ? 57.351  39.019  132.462 1.00 14.80 ? 215  HIS C O     1 
ATOM   7044  C  CB    . HIS K  3 215 ? 55.393  37.990  134.589 1.00 15.43 ? 215  HIS C CB    1 
ATOM   7045  C  CG    . HIS K  3 215 ? 54.109  37.717  135.291 1.00 15.57 ? 215  HIS C CG    1 
ATOM   7046  N  ND1   . HIS K  3 215 ? 53.011  37.140  134.689 1.00 17.64 ? 215  HIS C ND1   1 
ATOM   7047  C  CD2   . HIS K  3 215 ? 53.755  37.959  136.577 1.00 9.78  ? 215  HIS C CD2   1 
ATOM   7048  C  CE1   . HIS K  3 215 ? 52.031  37.036  135.578 1.00 13.87 ? 215  HIS C CE1   1 
ATOM   7049  N  NE2   . HIS K  3 215 ? 52.463  37.527  136.730 1.00 19.51 ? 215  HIS C NE2   1 
ATOM   7050  N  N     . ILE K  3 216 ? 57.770  40.280  134.287 1.00 12.58 ? 216  ILE C N     1 
ATOM   7051  C  CA    . ILE K  3 216 ? 59.207  40.442  133.993 1.00 12.52 ? 216  ILE C CA    1 
ATOM   7052  C  C     . ILE K  3 216 ? 59.917  40.085  135.294 1.00 13.95 ? 216  ILE C C     1 
ATOM   7053  O  O     . ILE K  3 216 ? 59.893  40.864  136.263 1.00 13.75 ? 216  ILE C O     1 
ATOM   7054  C  CB    . ILE K  3 216 ? 59.564  41.889  133.604 1.00 14.08 ? 216  ILE C CB    1 
ATOM   7055  C  CG1   . ILE K  3 216 ? 58.747  42.285  132.348 1.00 16.71 ? 216  ILE C CG1   1 
ATOM   7056  C  CG2   . ILE K  3 216 ? 61.071  42.001  133.340 1.00 15.11 ? 216  ILE C CG2   1 
ATOM   7057  C  CD1   . ILE K  3 216 ? 58.910  43.753  131.943 1.00 15.37 ? 216  ILE C CD1   1 
ATOM   7058  N  N     . VAL K  3 217 ? 60.535  38.913  135.325 1.00 12.42 ? 217  VAL C N     1 
ATOM   7059  C  CA    . VAL K  3 217 ? 61.201  38.474  136.563 1.00 12.20 ? 217  VAL C CA    1 
ATOM   7060  C  C     . VAL K  3 217 ? 62.606  37.947  136.302 1.00 14.42 ? 217  VAL C C     1 
ATOM   7061  O  O     . VAL K  3 217 ? 62.994  37.672  135.157 1.00 12.76 ? 217  VAL C O     1 
ATOM   7062  C  CB    . VAL K  3 217 ? 60.361  37.357  137.287 1.00 11.82 ? 217  VAL C CB    1 
ATOM   7063  C  CG1   . VAL K  3 217 ? 58.954  37.871  137.597 1.00 13.89 ? 217  VAL C CG1   1 
ATOM   7064  C  CG2   . VAL K  3 217 ? 60.270  36.087  136.413 1.00 13.82 ? 217  VAL C CG2   1 
ATOM   7065  N  N     . VAL K  3 218 ? 63.371  37.789  137.373 1.00 12.87 ? 218  VAL C N     1 
ATOM   7066  C  CA    . VAL K  3 218 ? 64.731  37.263  137.273 1.00 10.29 ? 218  VAL C CA    1 
ATOM   7067  C  C     . VAL K  3 218 ? 64.843  36.142  138.314 1.00 13.20 ? 218  VAL C C     1 
ATOM   7068  O  O     . VAL K  3 218 ? 64.349  36.290  139.443 1.00 14.94 ? 218  VAL C O     1 
ATOM   7069  C  CB    . VAL K  3 218 ? 65.771  38.324  137.643 1.00 14.46 ? 218  VAL C CB    1 
ATOM   7070  C  CG1   . VAL K  3 218 ? 67.160  37.707  137.588 1.00 13.47 ? 218  VAL C CG1   1 
ATOM   7071  C  CG2   . VAL K  3 218 ? 65.703  39.506  136.648 1.00 14.35 ? 218  VAL C CG2   1 
ATOM   7072  N  N     . VAL K  3 219 ? 65.443  35.027  137.908 1.00 11.39 ? 219  VAL C N     1 
ATOM   7073  C  CA    . VAL K  3 219 ? 65.679  33.909  138.836 1.00 12.22 ? 219  VAL C CA    1 
ATOM   7074  C  C     . VAL K  3 219 ? 67.203  33.783  138.937 1.00 15.63 ? 219  VAL C C     1 
ATOM   7075  O  O     . VAL K  3 219 ? 67.914  33.821  137.931 1.00 12.78 ? 219  VAL C O     1 
ATOM   7076  C  CB    . VAL K  3 219 ? 65.068  32.580  138.292 1.00 13.39 ? 219  VAL C CB    1 
ATOM   7077  C  CG1   . VAL K  3 219 ? 65.393  31.409  139.265 1.00 13.79 ? 219  VAL C CG1   1 
ATOM   7078  C  CG2   . VAL K  3 219 ? 63.553  32.740  138.069 1.00 14.57 ? 219  VAL C CG2   1 
ATOM   7079  N  N     . THR K  3 220 ? 67.732  33.605  140.145 1.00 13.60 ? 220  THR C N     1 
ATOM   7080  C  CA    . THR K  3 220 ? 69.186  33.523  140.267 1.00 13.67 ? 220  THR C CA    1 
ATOM   7081  C  C     . THR K  3 220 ? 69.643  32.572  141.357 1.00 15.30 ? 220  THR C C     1 
ATOM   7082  O  O     . THR K  3 220 ? 68.913  32.332  142.317 1.00 15.43 ? 220  THR C O     1 
ATOM   7083  C  CB    . THR K  3 220 ? 69.794  34.945  140.557 1.00 13.24 ? 220  THR C CB    1 
ATOM   7084  O  OG1   . THR K  3 220 ? 71.224  34.894  140.496 1.00 13.76 ? 220  THR C OG1   1 
ATOM   7085  C  CG2   . THR K  3 220 ? 69.356  35.475  141.947 1.00 17.50 ? 220  THR C CG2   1 
ATOM   7086  N  N     . ALA K  3 221 ? 70.851  32.051  141.185 1.00 13.73 ? 221  ALA C N     1 
ATOM   7087  C  CA    . ALA K  3 221 ? 71.450  31.184  142.207 1.00 13.88 ? 221  ALA C CA    1 
ATOM   7088  C  C     . ALA K  3 221 ? 72.597  31.955  142.890 1.00 17.58 ? 221  ALA C C     1 
ATOM   7089  O  O     . ALA K  3 221 ? 73.374  31.370  143.642 1.00 15.27 ? 221  ALA C O     1 
ATOM   7090  C  CB    . ALA K  3 221 ? 71.974  29.874  141.580 1.00 14.48 ? 221  ALA C CB    1 
ATOM   7091  N  N     . GLU K  3 222 ? 72.720  33.262  142.633 1.00 16.21 ? 222  GLU C N     1 
ATOM   7092  C  CA    . GLU K  3 222 ? 73.782  34.060  143.265 1.00 14.41 ? 222  GLU C CA    1 
ATOM   7093  C  C     . GLU K  3 222 ? 73.669  33.924  144.796 1.00 16.22 ? 222  GLU C C     1 
ATOM   7094  O  O     . GLU K  3 222 ? 72.611  34.165  145.358 1.00 13.77 ? 222  GLU C O     1 
ATOM   7095  C  CB    . GLU K  3 222 ? 73.642  35.544  142.866 1.00 12.04 ? 222  GLU C CB    1 
ATOM   7096  C  CG    . GLU K  3 222 ? 74.549  36.489  143.639 1.00 14.59 ? 222  GLU C CG    1 
ATOM   7097  C  CD    . GLU K  3 222 ? 76.035  36.110  143.574 1.00 15.66 ? 222  GLU C CD    1 
ATOM   7098  O  OE1   . GLU K  3 222 ? 76.731  36.293  144.611 1.00 16.37 ? 222  GLU C OE1   1 
ATOM   7099  O  OE2   . GLU K  3 222 ? 76.516  35.648  142.503 1.00 15.37 ? 222  GLU C OE2   1 
ATOM   7100  N  N     . PRO K  3 223 ? 74.762  33.561  145.489 1.00 15.67 ? 223  PRO C N     1 
ATOM   7101  C  CA    . PRO K  3 223 ? 74.662  33.418  146.954 1.00 15.12 ? 223  PRO C CA    1 
ATOM   7102  C  C     . PRO K  3 223 ? 74.714  34.689  147.801 1.00 16.22 ? 223  PRO C C     1 
ATOM   7103  O  O     . PRO K  3 223 ? 74.162  34.724  148.907 1.00 19.31 ? 223  PRO C O     1 
ATOM   7104  C  CB    . PRO K  3 223 ? 75.830  32.463  147.279 1.00 15.72 ? 223  PRO C CB    1 
ATOM   7105  C  CG    . PRO K  3 223 ? 76.884  32.889  146.302 1.00 19.65 ? 223  PRO C CG    1 
ATOM   7106  C  CD    . PRO K  3 223 ? 76.071  33.078  144.998 1.00 15.40 ? 223  PRO C CD    1 
ATOM   7107  N  N     . THR K  3 224 ? 75.336  35.753  147.301 1.00 14.34 ? 224  THR C N     1 
ATOM   7108  C  CA    . THR K  3 224 ? 75.471  36.939  148.126 1.00 15.97 ? 224  THR C CA    1 
ATOM   7109  C  C     . THR K  3 224 ? 74.387  37.991  147.998 1.00 19.21 ? 224  THR C C     1 
ATOM   7110  O  O     . THR K  3 224 ? 73.994  38.371  146.888 1.00 16.97 ? 224  THR C O     1 
ATOM   7111  C  CB    . THR K  3 224 ? 76.841  37.656  147.903 1.00 16.92 ? 224  THR C CB    1 
ATOM   7112  O  OG1   . THR K  3 224 ? 76.875  38.251  146.585 1.00 18.15 ? 224  THR C OG1   1 
ATOM   7113  C  CG2   . THR K  3 224 ? 78.023  36.664  148.027 1.00 16.84 ? 224  THR C CG2   1 
ATOM   7114  N  N     . PRO K  3 225 ? 73.866  38.467  149.136 1.00 18.65 ? 225  PRO C N     1 
ATOM   7115  C  CA    . PRO K  3 225 ? 72.835  39.504  149.075 1.00 18.30 ? 225  PRO C CA    1 
ATOM   7116  C  C     . PRO K  3 225 ? 73.338  40.744  148.308 1.00 18.97 ? 225  PRO C C     1 
ATOM   7117  O  O     . PRO K  3 225 ? 72.576  41.361  147.558 1.00 16.74 ? 225  PRO C O     1 
ATOM   7118  C  CB    . PRO K  3 225 ? 72.564  39.804  150.560 1.00 18.90 ? 225  PRO C CB    1 
ATOM   7119  C  CG    . PRO K  3 225 ? 72.665  38.425  151.162 1.00 17.12 ? 225  PRO C CG    1 
ATOM   7120  C  CD    . PRO K  3 225 ? 73.907  37.834  150.475 1.00 19.91 ? 225  PRO C CD    1 
ATOM   7121  N  N     . SER K  3 226 ? 74.615  41.110  148.481 1.00 15.90 ? 226  SER C N     1 
ATOM   7122  C  CA    . SER K  3 226 ? 75.136  42.292  147.798 1.00 15.86 ? 226  SER C CA    1 
ATOM   7123  C  C     . SER K  3 226 ? 74.977  42.170  146.281 1.00 15.86 ? 226  SER C C     1 
ATOM   7124  O  O     . SER K  3 226 ? 74.478  43.101  145.635 1.00 18.16 ? 226  SER C O     1 
ATOM   7125  C  CB    . SER K  3 226 ? 76.619  42.524  148.156 1.00 16.33 ? 226  SER C CB    1 
ATOM   7126  O  OG    . SER K  3 226 ? 77.401  41.387  147.862 1.00 26.03 ? 226  SER C OG    1 
ATOM   7127  N  N     . ARG K  3 227 ? 75.395  41.046  145.715 1.00 15.35 ? 227  ARG C N     1 
ATOM   7128  C  CA    . ARG K  3 227 ? 75.247  40.923  144.249 1.00 15.52 ? 227  ARG C CA    1 
ATOM   7129  C  C     . ARG K  3 227 ? 73.779  40.785  143.833 1.00 17.82 ? 227  ARG C C     1 
ATOM   7130  O  O     . ARG K  3 227 ? 73.368  41.317  142.799 1.00 15.64 ? 227  ARG C O     1 
ATOM   7131  C  CB    . ARG K  3 227 ? 76.088  39.750  143.710 1.00 14.46 ? 227  ARG C CB    1 
ATOM   7132  C  CG    . ARG K  3 227 ? 77.572  40.132  143.625 1.00 16.15 ? 227  ARG C CG    1 
ATOM   7133  C  CD    . ARG K  3 227 ? 78.492  38.945  143.440 1.00 16.12 ? 227  ARG C CD    1 
ATOM   7134  N  NE    . ARG K  3 227 ? 79.807  39.421  142.981 1.00 18.51 ? 227  ARG C NE    1 
ATOM   7135  C  CZ    . ARG K  3 227 ? 80.970  38.826  143.248 1.00 19.86 ? 227  ARG C CZ    1 
ATOM   7136  N  NH1   . ARG K  3 227 ? 81.007  37.707  143.987 1.00 18.96 ? 227  ARG C NH1   1 
ATOM   7137  N  NH2   . ARG K  3 227 ? 82.102  39.352  142.777 1.00 17.08 ? 227  ARG C NH2   1 
ATOM   7138  N  N     . ILE K  3 228 ? 72.980  40.083  144.625 1.00 14.52 ? 228  ILE C N     1 
ATOM   7139  C  CA    . ILE K  3 228 ? 71.567  39.958  144.285 1.00 15.43 ? 228  ILE C CA    1 
ATOM   7140  C  C     . ILE K  3 228 ? 70.937  41.365  144.243 1.00 16.69 ? 228  ILE C C     1 
ATOM   7141  O  O     . ILE K  3 228 ? 70.104  41.654  143.380 1.00 15.80 ? 228  ILE C O     1 
ATOM   7142  C  CB    . ILE K  3 228 ? 70.822  39.118  145.347 1.00 14.22 ? 228  ILE C CB    1 
ATOM   7143  C  CG1   . ILE K  3 228 ? 71.348  37.698  145.318 1.00 14.64 ? 228  ILE C CG1   1 
ATOM   7144  C  CG2   . ILE K  3 228 ? 69.286  39.226  145.125 1.00 16.25 ? 228  ILE C CG2   1 
ATOM   7145  C  CD1   . ILE K  3 228 ? 70.987  36.854  146.581 1.00 15.76 ? 228  ILE C CD1   1 
ATOM   7146  N  N     . SER K  3 229 ? 71.359  42.249  145.153 1.00 14.84 ? 229  SER C N     1 
ATOM   7147  C  CA    . SER K  3 229 ? 70.774  43.582  145.228 1.00 13.38 ? 229  SER C CA    1 
ATOM   7148  C  C     . SER K  3 229 ? 71.052  44.452  143.992 1.00 16.18 ? 229  SER C C     1 
ATOM   7149  O  O     . SER K  3 229 ? 70.313  45.411  143.734 1.00 16.31 ? 229  SER C O     1 
ATOM   7150  C  CB    . SER K  3 229 ? 71.244  44.305  146.526 1.00 15.77 ? 229  SER C CB    1 
ATOM   7151  O  OG    . SER K  3 229 ? 72.571  44.808  146.393 1.00 18.12 ? 229  SER C OG    1 
ATOM   7152  N  N     . SER K  3 230 ? 72.097  44.116  143.230 1.00 14.11 ? 230  SER C N     1 
ATOM   7153  C  CA    . SER K  3 230 ? 72.411  44.897  142.034 1.00 16.56 ? 230  SER C CA    1 
ATOM   7154  C  C     . SER K  3 230 ? 71.290  44.787  140.999 1.00 17.31 ? 230  SER C C     1 
ATOM   7155  O  O     . SER K  3 230 ? 71.215  45.627  140.093 1.00 16.94 ? 230  SER C O     1 
ATOM   7156  C  CB    . SER K  3 230 ? 73.762  44.477  141.420 1.00 18.34 ? 230  SER C CB    1 
ATOM   7157  O  OG    . SER K  3 230 ? 73.695  43.221  140.805 1.00 19.00 ? 230  SER C OG    1 
ATOM   7158  N  N     . ILE K  3 231 ? 70.420  43.780  141.130 1.00 13.52 ? 231  ILE C N     1 
ATOM   7159  C  CA    . ILE K  3 231 ? 69.290  43.683  140.196 1.00 15.63 ? 231  ILE C CA    1 
ATOM   7160  C  C     . ILE K  3 231 ? 67.944  43.739  140.911 1.00 16.98 ? 231  ILE C C     1 
ATOM   7161  O  O     . ILE K  3 231 ? 66.954  44.168  140.335 1.00 15.48 ? 231  ILE C O     1 
ATOM   7162  C  CB    . ILE K  3 231 ? 69.412  42.408  139.293 1.00 17.10 ? 231  ILE C CB    1 
ATOM   7163  C  CG1   . ILE K  3 231 ? 68.397  42.443  138.156 1.00 24.60 ? 231  ILE C CG1   1 
ATOM   7164  C  CG2   . ILE K  3 231 ? 69.246  41.154  140.097 1.00 18.80 ? 231  ILE C CG2   1 
ATOM   7165  C  CD1   . ILE K  3 231 ? 68.606  43.654  137.230 1.00 23.77 ? 231  ILE C CD1   1 
ATOM   7166  N  N     . ALA K  3 232 ? 67.900  43.340  142.191 1.00 14.36 ? 232  ALA C N     1 
ATOM   7167  C  CA    . ALA K  3 232 ? 66.618  43.330  142.918 1.00 13.55 ? 232  ALA C CA    1 
ATOM   7168  C  C     . ALA K  3 232 ? 66.154  44.680  143.473 1.00 14.15 ? 232  ALA C C     1 
ATOM   7169  O  O     . ALA K  3 232 ? 64.949  44.958  143.509 1.00 15.17 ? 232  ALA C O     1 
ATOM   7170  C  CB    . ALA K  3 232 ? 66.694  42.323  144.080 1.00 16.82 ? 232  ALA C CB    1 
ATOM   7171  N  N     . LEU K  3 233 ? 67.093  45.507  143.932 1.00 15.47 ? 233  LEU C N     1 
ATOM   7172  C  CA    . LEU K  3 233 ? 66.701  46.810  144.493 1.00 19.21 ? 233  LEU C CA    1 
ATOM   7173  C  C     . LEU K  3 233 ? 66.182  47.752  143.406 1.00 19.20 ? 233  LEU C C     1 
ATOM   7174  O  O     . LEU K  3 233 ? 66.625  47.702  142.262 1.00 17.06 ? 233  LEU C O     1 
ATOM   7175  C  CB    . LEU K  3 233 ? 67.891  47.464  145.231 1.00 17.77 ? 233  LEU C CB    1 
ATOM   7176  C  CG    . LEU K  3 233 ? 68.305  46.756  146.527 1.00 18.58 ? 233  LEU C CG    1 
ATOM   7177  C  CD1   . LEU K  3 233 ? 69.536  47.458  147.076 1.00 21.19 ? 233  LEU C CD1   1 
ATOM   7178  C  CD2   . LEU K  3 233 ? 67.152  46.771  147.554 1.00 20.70 ? 233  LEU C CD2   1 
ATOM   7179  N  N     . GLY K  3 234 ? 65.242  48.614  143.778 1.00 21.14 ? 234  GLY C N     1 
ATOM   7180  C  CA    . GLY K  3 234 ? 64.698  49.545  142.806 1.00 21.55 ? 234  GLY C CA    1 
ATOM   7181  C  C     . GLY K  3 234 ? 63.467  48.952  142.150 1.00 21.22 ? 234  GLY C C     1 
ATOM   7182  O  O     . GLY K  3 234 ? 63.199  47.754  142.286 1.00 19.55 ? 234  GLY C O     1 
ATOM   7183  N  N     . THR K  3 235 ? 62.715  49.797  141.453 1.00 20.32 ? 235  THR C N     1 
ATOM   7184  C  CA    . THR K  3 235 ? 61.495  49.367  140.765 1.00 19.19 ? 235  THR C CA    1 
ATOM   7185  C  C     . THR K  3 235 ? 61.434  50.025  139.409 1.00 17.13 ? 235  THR C C     1 
ATOM   7186  O  O     . THR K  3 235 ? 62.130  51.017  139.166 1.00 20.80 ? 235  THR C O     1 
ATOM   7187  C  CB    . THR K  3 235 ? 60.209  49.794  141.521 1.00 18.09 ? 235  THR C CB    1 
ATOM   7188  O  OG1   . THR K  3 235 ? 60.219  51.216  141.725 1.00 19.50 ? 235  THR C OG1   1 
ATOM   7189  C  CG2   . THR K  3 235 ? 60.107  49.069  142.867 1.00 19.76 ? 235  THR C CG2   1 
ATOM   7190  N  N     . GLY K  3 236 ? 60.624  49.464  138.514 1.00 15.82 ? 236  GLY C N     1 
ATOM   7191  C  CA    . GLY K  3 236 ? 60.449  50.085  137.204 1.00 16.38 ? 236  GLY C CA    1 
ATOM   7192  C  C     . GLY K  3 236 ? 60.756  49.180  136.025 1.00 16.66 ? 236  GLY C C     1 
ATOM   7193  O  O     . GLY K  3 236 ? 60.104  49.279  134.981 1.00 18.44 ? 236  GLY C O     1 
ATOM   7194  N  N     . GLU K  3 237 ? 61.746  48.304  136.177 1.00 15.83 ? 237  GLU C N     1 
ATOM   7195  C  CA    . GLU K  3 237 ? 62.136  47.389  135.101 1.00 16.43 ? 237  GLU C CA    1 
ATOM   7196  C  C     . GLU K  3 237 ? 61.797  45.934  135.430 1.00 17.60 ? 237  GLU C C     1 
ATOM   7197  O  O     . GLU K  3 237 ? 61.265  45.198  134.594 1.00 17.64 ? 237  GLU C O     1 
ATOM   7198  C  CB    . GLU K  3 237 ? 63.657  47.448  134.856 1.00 14.56 ? 237  GLU C CB    1 
ATOM   7199  C  CG    . GLU K  3 237 ? 64.241  48.839  134.569 1.00 24.30 ? 237  GLU C CG    1 
ATOM   7200  C  CD    . GLU K  3 237 ? 64.688  49.614  135.810 1.00 28.34 ? 237  GLU C CD    1 
ATOM   7201  O  OE1   . GLU K  3 237 ? 65.004  49.029  136.881 1.00 22.56 ? 237  GLU C OE1   1 
ATOM   7202  O  OE2   . GLU K  3 237 ? 64.747  50.850  135.695 1.00 31.66 ? 237  GLU C OE2   1 
ATOM   7203  N  N     . ILE K  3 238 ? 62.140  45.523  136.651 1.00 15.38 ? 238  ILE C N     1 
ATOM   7204  C  CA    . ILE K  3 238 ? 61.960  44.139  137.112 1.00 14.27 ? 238  ILE C CA    1 
ATOM   7205  C  C     . ILE K  3 238 ? 60.850  44.030  138.153 1.00 14.12 ? 238  ILE C C     1 
ATOM   7206  O  O     . ILE K  3 238 ? 60.857  44.765  139.150 1.00 15.52 ? 238  ILE C O     1 
ATOM   7207  C  CB    . ILE K  3 238 ? 63.277  43.647  137.732 1.00 14.57 ? 238  ILE C CB    1 
ATOM   7208  C  CG1   . ILE K  3 238 ? 64.400  43.774  136.670 1.00 16.07 ? 238  ILE C CG1   1 
ATOM   7209  C  CG2   . ILE K  3 238 ? 63.124  42.210  138.259 1.00 15.66 ? 238  ILE C CG2   1 
ATOM   7210  C  CD1   . ILE K  3 238 ? 65.721  43.627  137.252 1.00 24.02 ? 238  ILE C CD1   1 
ATOM   7211  N  N     . ASP K  3 239 ? 59.911  43.119  137.922 1.00 12.64 ? 239  ASP C N     1 
ATOM   7212  C  CA    . ASP K  3 239 ? 58.769  42.953  138.841 1.00 11.26 ? 239  ASP C CA    1 
ATOM   7213  C  C     . ASP K  3 239 ? 59.251  42.455  140.195 1.00 13.97 ? 239  ASP C C     1 
ATOM   7214  O  O     . ASP K  3 239 ? 58.816  42.960  141.239 1.00 13.70 ? 239  ASP C O     1 
ATOM   7215  C  CB    . ASP K  3 239 ? 57.739  41.933  138.313 1.00 13.44 ? 239  ASP C CB    1 
ATOM   7216  C  CG    . ASP K  3 239 ? 57.080  42.339  136.981 1.00 14.05 ? 239  ASP C CG    1 
ATOM   7217  O  OD1   . ASP K  3 239 ? 57.306  43.452  136.491 1.00 14.83 ? 239  ASP C OD1   1 
ATOM   7218  O  OD2   . ASP K  3 239 ? 56.332  41.513  136.438 1.00 14.99 ? 239  ASP C OD2   1 
ATOM   7219  N  N     . CYS K  3 240 ? 60.140  41.465  140.169 1.00 11.49 ? 240  CYS C N     1 
ATOM   7220  C  CA    . CYS K  3 240 ? 60.645  40.862  141.403 1.00 14.54 ? 240  CYS C CA    1 
ATOM   7221  C  C     . CYS K  3 240 ? 61.749  39.862  141.019 1.00 15.07 ? 240  CYS C C     1 
ATOM   7222  O  O     . CYS K  3 240 ? 61.789  39.364  139.878 1.00 13.70 ? 240  CYS C O     1 
ATOM   7223  C  CB    . CYS K  3 240 ? 59.505  40.113  142.085 1.00 12.05 ? 240  CYS C CB    1 
ATOM   7224  S  SG    . CYS K  3 240 ? 59.856  39.554  143.817 1.00 15.66 ? 240  CYS C SG    1 
ATOM   7225  N  N     . VAL K  3 241 ? 62.610  39.525  141.977 1.00 13.11 ? 241  VAL C N     1 
ATOM   7226  C  CA    . VAL K  3 241 ? 63.683  38.561  141.761 1.00 12.26 ? 241  VAL C CA    1 
ATOM   7227  C  C     . VAL K  3 241 ? 63.376  37.333  142.638 1.00 13.90 ? 241  VAL C C     1 
ATOM   7228  O  O     . VAL K  3 241 ? 62.816  37.472  143.719 1.00 14.06 ? 241  VAL C O     1 
ATOM   7229  C  CB    . VAL K  3 241 ? 65.043  39.167  142.149 1.00 15.22 ? 241  VAL C CB    1 
ATOM   7230  C  CG1   . VAL K  3 241 ? 66.169  38.130  141.984 1.00 12.95 ? 241  VAL C CG1   1 
ATOM   7231  C  CG2   . VAL K  3 241 ? 65.322  40.386  141.243 1.00 13.74 ? 241  VAL C CG2   1 
ATOM   7232  N  N     . TYR K  3 242 ? 63.722  36.151  142.146 1.00 13.27 ? 242  TYR C N     1 
ATOM   7233  C  CA    . TYR K  3 242 ? 63.458  34.905  142.871 1.00 13.54 ? 242  TYR C CA    1 
ATOM   7234  C  C     . TYR K  3 242 ? 64.766  34.154  143.037 1.00 15.74 ? 242  TYR C C     1 
ATOM   7235  O  O     . TYR K  3 242 ? 65.489  33.926  142.067 1.00 14.00 ? 242  TYR C O     1 
ATOM   7236  C  CB    . TYR K  3 242 ? 62.470  34.043  142.086 1.00 12.92 ? 242  TYR C CB    1 
ATOM   7237  C  CG    . TYR K  3 242 ? 61.136  34.740  141.919 1.00 12.60 ? 242  TYR C CG    1 
ATOM   7238  C  CD1   . TYR K  3 242 ? 60.984  35.775  140.982 1.00 13.61 ? 242  TYR C CD1   1 
ATOM   7239  C  CD2   . TYR K  3 242 ? 60.044  34.421  142.744 1.00 13.09 ? 242  TYR C CD2   1 
ATOM   7240  C  CE1   . TYR K  3 242 ? 59.779  36.473  140.869 1.00 11.76 ? 242  TYR C CE1   1 
ATOM   7241  C  CE2   . TYR K  3 242 ? 58.828  35.108  142.643 1.00 12.03 ? 242  TYR C CE2   1 
ATOM   7242  C  CZ    . TYR K  3 242 ? 58.706  36.140  141.688 1.00 10.87 ? 242  TYR C CZ    1 
ATOM   7243  O  OH    . TYR K  3 242 ? 57.528  36.809  141.585 1.00 12.52 ? 242  TYR C OH    1 
ATOM   7244  N  N     . HIS K  3 243 ? 65.077  33.779  144.279 1.00 14.04 ? 243  HIS C N     1 
ATOM   7245  C  CA    . HIS K  3 243 ? 66.322  33.075  144.599 1.00 14.19 ? 243  HIS C CA    1 
ATOM   7246  C  C     . HIS K  3 243 ? 66.127  31.556  144.587 1.00 14.02 ? 243  HIS C C     1 
ATOM   7247  O  O     . HIS K  3 243 ? 65.106  31.062  145.056 1.00 15.11 ? 243  HIS C O     1 
ATOM   7248  C  CB    . HIS K  3 243 ? 66.807  33.528  145.989 1.00 14.66 ? 243  HIS C CB    1 
ATOM   7249  C  CG    . HIS K  3 243 ? 68.229  33.160  146.271 1.00 13.98 ? 243  HIS C CG    1 
ATOM   7250  N  ND1   . HIS K  3 243 ? 68.577  32.010  146.949 1.00 15.82 ? 243  HIS C ND1   1 
ATOM   7251  C  CD2   . HIS K  3 243 ? 69.393  33.740  145.887 1.00 17.16 ? 243  HIS C CD2   1 
ATOM   7252  C  CE1   . HIS K  3 243 ? 69.894  31.893  146.962 1.00 16.23 ? 243  HIS C CE1   1 
ATOM   7253  N  NE2   . HIS K  3 243 ? 70.415  32.931  146.325 1.00 17.52 ? 243  HIS C NE2   1 
ATOM   7254  N  N     . PHE K  3 244 ? 67.117  30.818  144.080 1.00 14.13 ? 244  PHE C N     1 
ATOM   7255  C  CA    . PHE K  3 244 ? 66.980  29.373  143.973 1.00 12.98 ? 244  PHE C CA    1 
ATOM   7256  C  C     . PHE K  3 244 ? 66.932  28.610  145.296 1.00 14.47 ? 244  PHE C C     1 
ATOM   7257  O  O     . PHE K  3 244 ? 66.492  27.473  145.314 1.00 18.14 ? 244  PHE C O     1 
ATOM   7258  C  CB    . PHE K  3 244 ? 68.088  28.771  143.091 1.00 15.63 ? 244  PHE C CB    1 
ATOM   7259  C  CG    . PHE K  3 244 ? 69.317  28.340  143.848 1.00 17.32 ? 244  PHE C CG    1 
ATOM   7260  C  CD1   . PHE K  3 244 ? 69.753  27.016  143.766 1.00 15.77 ? 244  PHE C CD1   1 
ATOM   7261  C  CD2   . PHE K  3 244 ? 70.049  29.242  144.597 1.00 14.54 ? 244  PHE C CD2   1 
ATOM   7262  C  CE1   . PHE K  3 244 ? 70.927  26.606  144.429 1.00 14.50 ? 244  PHE C CE1   1 
ATOM   7263  C  CE2   . PHE K  3 244 ? 71.228  28.831  145.272 1.00 18.00 ? 244  PHE C CE2   1 
ATOM   7264  C  CZ    . PHE K  3 244 ? 71.652  27.509  145.171 1.00 16.43 ? 244  PHE C CZ    1 
ATOM   7265  N  N     . ALA K  3 245 ? 67.356  29.250  146.369 1.00 14.50 ? 245  ALA C N     1 
ATOM   7266  C  CA    . ALA K  3 245 ? 67.363  28.570  147.687 1.00 15.56 ? 245  ALA C CA    1 
ATOM   7267  C  C     . ALA K  3 245 ? 67.255  29.638  148.774 1.00 16.17 ? 245  ALA C C     1 
ATOM   7268  O  O     . ALA K  3 245 ? 68.156  29.822  149.608 1.00 17.64 ? 245  ALA C O     1 
ATOM   7269  C  CB    . ALA K  3 245 ? 68.678  27.748  147.837 1.00 16.40 ? 245  ALA C CB    1 
ATOM   7270  N  N     . LEU K  3 246 ? 66.126  30.332  148.787 1.00 15.48 ? 246  LEU C N     1 
ATOM   7271  C  CA    . LEU K  3 246 ? 65.973  31.439  149.713 1.00 14.77 ? 246  LEU C CA    1 
ATOM   7272  C  C     . LEU K  3 246 ? 65.992  31.042  151.190 1.00 16.14 ? 246  LEU C C     1 
ATOM   7273  O  O     . LEU K  3 246 ? 66.627  31.728  151.982 1.00 17.57 ? 246  LEU C O     1 
ATOM   7274  C  CB    . LEU K  3 246 ? 64.689  32.230  149.417 1.00 15.74 ? 246  LEU C CB    1 
ATOM   7275  C  CG    . LEU K  3 246 ? 64.632  33.596  150.121 1.00 18.12 ? 246  LEU C CG    1 
ATOM   7276  C  CD1   . LEU K  3 246 ? 65.356  34.689  149.323 1.00 17.10 ? 246  LEU C CD1   1 
ATOM   7277  C  CD2   . LEU K  3 246 ? 63.181  33.998  150.298 1.00 17.81 ? 246  LEU C CD2   1 
ATOM   7278  N  N     . TYR K  3 247 ? 65.288  29.964  151.538 1.00 19.95 ? 247  TYR C N     1 
ATOM   7279  C  CA    . TYR K  3 247 ? 65.212  29.544  152.952 1.00 19.35 ? 247  TYR C CA    1 
ATOM   7280  C  C     . TYR K  3 247 ? 66.588  29.173  153.498 1.00 20.60 ? 247  TYR C C     1 
ATOM   7281  O  O     . TYR K  3 247 ? 66.944  29.545  154.626 1.00 22.32 ? 247  TYR C O     1 
ATOM   7282  C  CB    . TYR K  3 247 ? 64.273  28.360  153.104 1.00 18.39 ? 247  TYR C CB    1 
ATOM   7283  C  CG    . TYR K  3 247 ? 62.954  28.567  152.410 1.00 16.42 ? 247  TYR C CG    1 
ATOM   7284  C  CD1   . TYR K  3 247 ? 62.321  27.502  151.782 1.00 18.43 ? 247  TYR C CD1   1 
ATOM   7285  C  CD2   . TYR K  3 247 ? 62.358  29.825  152.365 1.00 18.76 ? 247  TYR C CD2   1 
ATOM   7286  C  CE1   . TYR K  3 247 ? 61.122  27.668  151.108 1.00 18.83 ? 247  TYR C CE1   1 
ATOM   7287  C  CE2   . TYR K  3 247 ? 61.132  30.008  151.688 1.00 19.54 ? 247  TYR C CE2   1 
ATOM   7288  C  CZ    . TYR K  3 247 ? 60.541  28.926  151.070 1.00 18.76 ? 247  TYR C CZ    1 
ATOM   7289  O  OH    . TYR K  3 247 ? 59.358  29.060  150.385 1.00 20.60 ? 247  TYR C OH    1 
ATOM   7290  N  N     . GLU K  3 248 ? 67.356  28.485  152.670 1.00 20.23 ? 248  GLU C N     1 
ATOM   7291  C  CA    . GLU K  3 248 ? 68.702  28.071  153.037 1.00 17.58 ? 248  GLU C CA    1 
ATOM   7292  C  C     . GLU K  3 248 ? 69.613  29.299  153.137 1.00 21.14 ? 248  GLU C C     1 
ATOM   7293  O  O     . GLU K  3 248 ? 70.448  29.401  154.043 1.00 19.42 ? 248  GLU C O     1 
ATOM   7294  C  CB    . GLU K  3 248 ? 69.225  27.074  151.999 1.00 18.37 ? 248  GLU C CB    1 
ATOM   7295  C  CG    . GLU K  3 248 ? 68.438  25.763  151.937 1.00 18.77 ? 248  GLU C CG    1 
ATOM   7296  C  CD    . GLU K  3 248 ? 67.123  25.870  151.160 1.00 22.97 ? 248  GLU C CD    1 
ATOM   7297  O  OE1   . GLU K  3 248 ? 66.855  26.938  150.547 1.00 19.62 ? 248  GLU C OE1   1 
ATOM   7298  O  OE2   . GLU K  3 248 ? 66.364  24.879  151.152 1.00 22.52 ? 248  GLU C OE2   1 
ATOM   7299  N  N     . LEU K  3 249 ? 69.487  30.242  152.196 1.00 16.82 ? 249  LEU C N     1 
ATOM   7300  C  CA    . LEU K  3 249 ? 70.285  31.472  152.251 1.00 16.10 ? 249  LEU C CA    1 
ATOM   7301  C  C     . LEU K  3 249 ? 70.011  32.200  153.569 1.00 18.20 ? 249  LEU C C     1 
ATOM   7302  O  O     . LEU K  3 249 ? 70.938  32.677  154.231 1.00 20.38 ? 249  LEU C O     1 
ATOM   7303  C  CB    . LEU K  3 249 ? 69.904  32.423  151.088 1.00 15.59 ? 249  LEU C CB    1 
ATOM   7304  C  CG    . LEU K  3 249 ? 70.511  33.831  151.101 1.00 15.96 ? 249  LEU C CG    1 
ATOM   7305  C  CD1   . LEU K  3 249 ? 72.041  33.793  151.173 1.00 17.98 ? 249  LEU C CD1   1 
ATOM   7306  C  CD2   . LEU K  3 249 ? 70.033  34.582  149.812 1.00 18.37 ? 249  LEU C CD2   1 
ATOM   7307  N  N     . GLU K  3 250 ? 68.737  32.276  153.955 1.00 18.83 ? 250  GLU C N     1 
ATOM   7308  C  CA    . GLU K  3 250 ? 68.385  32.961  155.199 1.00 20.07 ? 250  GLU C CA    1 
ATOM   7309  C  C     . GLU K  3 250 ? 68.997  32.246  156.404 1.00 22.58 ? 250  GLU C C     1 
ATOM   7310  O  O     . GLU K  3 250 ? 69.563  32.896  157.271 1.00 24.97 ? 250  GLU C O     1 
ATOM   7311  C  CB    . GLU K  3 250 ? 66.859  33.027  155.366 1.00 22.49 ? 250  GLU C CB    1 
ATOM   7312  C  CG    . GLU K  3 250 ? 66.411  33.781  156.612 1.00 26.91 ? 250  GLU C CG    1 
ATOM   7313  C  CD    . GLU K  3 250 ? 64.895  33.698  156.849 1.00 31.27 ? 250  GLU C CD    1 
ATOM   7314  O  OE1   . GLU K  3 250 ? 64.233  32.747  156.362 1.00 34.09 ? 250  GLU C OE1   1 
ATOM   7315  O  OE2   . GLU K  3 250 ? 64.370  34.593  157.542 1.00 31.86 ? 250  GLU C OE2   1 
ATOM   7316  N  N     . GLN K  3 251 ? 68.885  30.925  156.433 1.00 23.53 ? 251  GLN C N     1 
ATOM   7317  C  CA    . GLN K  3 251 ? 69.416  30.137  157.562 1.00 25.77 ? 251  GLN C CA    1 
ATOM   7318  C  C     . GLN K  3 251 ? 70.929  30.323  157.719 1.00 27.85 ? 251  GLN C C     1 
ATOM   7319  O  O     . GLN K  3 251 ? 71.424  30.574  158.825 1.00 27.40 ? 251  GLN C O     1 
ATOM   7320  C  CB    . GLN K  3 251 ? 69.074  28.655  157.368 1.00 27.22 ? 251  GLN C CB    1 
ATOM   7321  C  CG    . GLN K  3 251 ? 69.163  27.780  158.636 1.00 37.01 ? 251  GLN C CG    1 
ATOM   7322  C  CD    . GLN K  3 251 ? 68.815  26.318  158.364 1.00 42.49 ? 251  GLN C CD    1 
ATOM   7323  O  OE1   . GLN K  3 251 ? 67.846  26.013  157.655 1.00 44.97 ? 251  GLN C OE1   1 
ATOM   7324  N  NE2   . GLN K  3 251 ? 69.600  25.404  158.934 1.00 46.85 ? 251  GLN C NE2   1 
ATOM   7325  N  N     . ILE K  3 252 ? 71.677  30.246  156.619 1.00 23.96 ? 252  ILE C N     1 
ATOM   7326  C  CA    . ILE K  3 252 ? 73.130  30.394  156.709 1.00 24.35 ? 252  ILE C CA    1 
ATOM   7327  C  C     . ILE K  3 252 ? 73.539  31.813  157.081 1.00 24.58 ? 252  ILE C C     1 
ATOM   7328  O  O     . ILE K  3 252 ? 74.541  32.013  157.788 1.00 23.74 ? 252  ILE C O     1 
ATOM   7329  C  CB    . ILE K  3 252 ? 73.830  29.982  155.405 1.00 27.92 ? 252  ILE C CB    1 
ATOM   7330  C  CG1   . ILE K  3 252 ? 73.403  30.906  154.274 1.00 35.26 ? 252  ILE C CG1   1 
ATOM   7331  C  CG2   . ILE K  3 252 ? 73.443  28.562  155.038 1.00 33.24 ? 252  ILE C CG2   1 
ATOM   7332  C  CD1   . ILE K  3 252 ? 74.034  30.549  152.972 1.00 44.50 ? 252  ILE C CD1   1 
ATOM   7333  N  N     . LEU K  3 253 ? 72.773  32.810  156.618 1.00 23.78 ? 253  LEU C N     1 
ATOM   7334  C  CA    . LEU K  3 253 ? 73.083  34.197  156.961 1.00 24.55 ? 253  LEU C CA    1 
ATOM   7335  C  C     . LEU K  3 253 ? 72.916  34.384  158.471 1.00 26.62 ? 253  LEU C C     1 
ATOM   7336  O  O     . LEU K  3 253 ? 73.668  35.124  159.092 1.00 27.26 ? 253  LEU C O     1 
ATOM   7337  C  CB    . LEU K  3 253 ? 72.157  35.170  156.226 1.00 24.06 ? 253  LEU C CB    1 
ATOM   7338  C  CG    . LEU K  3 253 ? 72.481  35.339  154.726 1.00 20.86 ? 253  LEU C CG    1 
ATOM   7339  C  CD1   . LEU K  3 253 ? 71.391  36.190  154.109 1.00 18.10 ? 253  LEU C CD1   1 
ATOM   7340  C  CD2   . LEU K  3 253 ? 73.829  35.986  154.512 1.00 20.76 ? 253  LEU C CD2   1 
ATOM   7341  N  N     . GLN K  3 254 ? 71.926  33.704  159.031 1.00 29.02 ? 254  GLN C N     1 
ATOM   7342  C  CA    . GLN K  3 254 ? 71.661  33.767  160.470 1.00 31.79 ? 254  GLN C CA    1 
ATOM   7343  C  C     . GLN K  3 254 ? 72.819  33.116  161.240 1.00 33.17 ? 254  GLN C C     1 
ATOM   7344  O  O     . GLN K  3 254 ? 73.260  33.631  162.266 1.00 35.46 ? 254  GLN C O     1 
ATOM   7345  C  CB    . GLN K  3 254 ? 70.352  33.042  160.792 1.00 35.43 ? 254  GLN C CB    1 
ATOM   7346  C  CG    . GLN K  3 254 ? 69.103  33.784  160.332 1.00 39.91 ? 254  GLN C CG    1 
ATOM   7347  C  CD    . GLN K  3 254 ? 68.863  35.062  161.120 1.00 44.46 ? 254  GLN C CD    1 
ATOM   7348  O  OE1   . GLN K  3 254 ? 69.782  35.615  161.727 1.00 46.56 ? 254  GLN C OE1   1 
ATOM   7349  N  NE2   . GLN K  3 254 ? 67.625  35.547  161.102 1.00 47.25 ? 254  GLN C NE2   1 
ATOM   7350  N  N     . SER K  3 255 ? 73.331  32.004  160.719 1.00 32.15 ? 255  SER C N     1 
ATOM   7351  C  CA    . SER K  3 255 ? 74.418  31.280  161.379 1.00 32.49 ? 255  SER C CA    1 
ATOM   7352  C  C     . SER K  3 255 ? 75.783  31.939  161.290 1.00 32.54 ? 255  SER C C     1 
ATOM   7353  O  O     . SER K  3 255 ? 76.578  31.854  162.230 1.00 32.39 ? 255  SER C O     1 
ATOM   7354  C  CB    . SER K  3 255 ? 74.545  29.868  160.812 1.00 31.85 ? 255  SER C CB    1 
ATOM   7355  O  OG    . SER K  3 255 ? 73.304  29.196  160.823 1.00 39.17 ? 255  SER C OG    1 
ATOM   7356  N  N     . LEU K  3 256 ? 76.059  32.600  160.173 1.00 27.18 ? 256  LEU C N     1 
ATOM   7357  C  CA    . LEU K  3 256 ? 77.351  33.230  159.958 1.00 29.70 ? 256  LEU C CA    1 
ATOM   7358  C  C     . LEU K  3 256 ? 77.674  34.597  160.563 1.00 30.12 ? 256  LEU C C     1 
ATOM   7359  O  O     . LEU K  3 256 ? 78.829  34.994  160.556 1.00 34.94 ? 256  LEU C O     1 
ATOM   7360  C  CB    . LEU K  3 256 ? 77.649  33.274  158.459 1.00 26.99 ? 256  LEU C CB    1 
ATOM   7361  C  CG    . LEU K  3 256 ? 77.839  31.893  157.836 1.00 29.21 ? 256  LEU C CG    1 
ATOM   7362  C  CD1   . LEU K  3 256 ? 78.005  32.010  156.336 1.00 29.53 ? 256  LEU C CD1   1 
ATOM   7363  C  CD2   . LEU K  3 256 ? 79.070  31.242  158.443 1.00 33.61 ? 256  LEU C CD2   1 
ATOM   7364  N  N     . ASN K  3 257 ? 76.698  35.341  161.058 1.00 35.22 ? 257  ASN C N     1 
ATOM   7365  C  CA    . ASN K  3 257 ? 77.058  36.635  161.649 1.00 35.57 ? 257  ASN C CA    1 
ATOM   7366  C  C     . ASN K  3 257 ? 77.560  37.688  160.633 1.00 34.45 ? 257  ASN C C     1 
ATOM   7367  O  O     . ASN K  3 257 ? 78.421  38.514  160.954 1.00 35.95 ? 257  ASN C O     1 
ATOM   7368  C  CB    . ASN K  3 257 ? 78.121  36.389  162.751 1.00 38.69 ? 257  ASN C CB    1 
ATOM   7369  C  CG    . ASN K  3 257 ? 78.507  37.647  163.510 1.00 39.74 ? 257  ASN C CG    1 
ATOM   7370  O  OD1   . ASN K  3 257 ? 77.662  38.489  163.805 1.00 41.98 ? 257  ASN C OD1   1 
ATOM   7371  N  ND2   . ASN K  3 257 ? 79.794  37.764  163.857 1.00 42.13 ? 257  ASN C ND2   1 
ATOM   7372  N  N     . TYR K  3 258 ? 77.069  37.638  159.393 1.00 28.75 ? 258  TYR C N     1 
ATOM   7373  C  CA    . TYR K  3 258 ? 77.443  38.665  158.403 1.00 25.70 ? 258  TYR C CA    1 
ATOM   7374  C  C     . TYR K  3 258 ? 76.241  39.603  158.556 1.00 23.74 ? 258  TYR C C     1 
ATOM   7375  O  O     . TYR K  3 258 ? 75.239  39.476  157.852 1.00 25.48 ? 258  TYR C O     1 
ATOM   7376  C  CB    . TYR K  3 258 ? 77.494  38.072  156.979 1.00 25.05 ? 258  TYR C CB    1 
ATOM   7377  C  CG    . TYR K  3 258 ? 78.624  37.095  156.703 1.00 28.20 ? 258  TYR C CG    1 
ATOM   7378  C  CD1   . TYR K  3 258 ? 78.478  36.084  155.761 1.00 27.66 ? 258  TYR C CD1   1 
ATOM   7379  C  CD2   . TYR K  3 258 ? 79.847  37.184  157.380 1.00 29.84 ? 258  TYR C CD2   1 
ATOM   7380  C  CE1   . TYR K  3 258 ? 79.512  35.184  155.500 1.00 27.16 ? 258  TYR C CE1   1 
ATOM   7381  C  CE2   . TYR K  3 258 ? 80.877  36.295  157.119 1.00 26.79 ? 258  TYR C CE2   1 
ATOM   7382  C  CZ    . TYR K  3 258 ? 80.703  35.299  156.183 1.00 26.84 ? 258  TYR C CZ    1 
ATOM   7383  O  OH    . TYR K  3 258 ? 81.736  34.433  155.921 1.00 32.67 ? 258  TYR C OH    1 
ATOM   7384  N  N     . GLU K  3 259 ? 76.319  40.536  159.495 1.00 24.35 ? 259  GLU C N     1 
ATOM   7385  C  CA    . GLU K  3 259 ? 75.178  41.396  159.764 1.00 27.01 ? 259  GLU C CA    1 
ATOM   7386  C  C     . GLU K  3 259 ? 74.747  42.351  158.668 1.00 25.82 ? 259  GLU C C     1 
ATOM   7387  O  O     . GLU K  3 259 ? 73.560  42.652  158.551 1.00 28.36 ? 259  GLU C O     1 
ATOM   7388  C  CB    . GLU K  3 259 ? 75.368  42.183  161.067 1.00 29.48 ? 259  GLU C CB    1 
ATOM   7389  C  CG    . GLU K  3 259 ? 75.389  41.339  162.353 1.00 40.38 ? 259  GLU C CG    1 
ATOM   7390  C  CD    . GLU K  3 259 ? 74.285  40.288  162.428 1.00 47.46 ? 259  GLU C CD    1 
ATOM   7391  O  OE1   . GLU K  3 259 ? 73.207  40.510  161.837 1.00 57.74 ? 259  GLU C OE1   1 
ATOM   7392  O  OE2   . GLU K  3 259 ? 74.486  39.241  163.096 1.00 53.48 ? 259  GLU C OE2   1 
ATOM   7393  N  N     . ASP K  3 260 ? 75.697  42.850  157.878 1.00 26.36 ? 260  ASP C N     1 
ATOM   7394  C  CA    . ASP K  3 260 ? 75.336  43.768  156.798 1.00 27.77 ? 260  ASP C CA    1 
ATOM   7395  C  C     . ASP K  3 260 ? 74.561  42.992  155.718 1.00 25.29 ? 260  ASP C C     1 
ATOM   7396  O  O     . ASP K  3 260 ? 73.559  43.491  155.190 1.00 23.54 ? 260  ASP C O     1 
ATOM   7397  C  CB    . ASP K  3 260 ? 76.601  44.416  156.209 1.00 30.16 ? 260  ASP C CB    1 
ATOM   7398  C  CG    . ASP K  3 260 ? 77.621  43.393  155.779 1.00 35.29 ? 260  ASP C CG    1 
ATOM   7399  O  OD1   . ASP K  3 260 ? 77.931  42.477  156.583 1.00 32.61 ? 260  ASP C OD1   1 
ATOM   7400  O  OD2   . ASP K  3 260 ? 78.114  43.492  154.632 1.00 40.19 ? 260  ASP C OD2   1 
ATOM   7401  N  N     . ALA K  3 261 ? 75.006  41.771  155.434 1.00 23.84 ? 261  ALA C N     1 
ATOM   7402  C  CA    . ALA K  3 261 ? 74.370  40.906  154.423 1.00 23.13 ? 261  ALA C CA    1 
ATOM   7403  C  C     . ALA K  3 261 ? 72.978  40.489  154.884 1.00 24.52 ? 261  ALA C C     1 
ATOM   7404  O  O     . ALA K  3 261 ? 72.029  40.431  154.090 1.00 21.68 ? 261  ALA C O     1 
ATOM   7405  C  CB    . ALA K  3 261 ? 75.229  39.660  154.168 1.00 20.85 ? 261  ALA C CB    1 
ATOM   7406  N  N     . LEU K  3 262 ? 72.851  40.194  156.176 1.00 22.79 ? 262  LEU C N     1 
ATOM   7407  C  CA    . LEU K  3 262 ? 71.566  39.794  156.731 1.00 24.17 ? 262  LEU C CA    1 
ATOM   7408  C  C     . LEU K  3 262 ? 70.591  40.967  156.617 1.00 23.21 ? 262  LEU C C     1 
ATOM   7409  O  O     . LEU K  3 262 ? 69.429  40.797  156.212 1.00 22.30 ? 262  LEU C O     1 
ATOM   7410  C  CB    . LEU K  3 262 ? 71.733  39.397  158.203 1.00 25.92 ? 262  LEU C CB    1 
ATOM   7411  C  CG    . LEU K  3 262 ? 71.259  38.029  158.687 1.00 36.43 ? 262  LEU C CG    1 
ATOM   7412  C  CD1   . LEU K  3 262 ? 71.092  38.116  160.204 1.00 37.47 ? 262  LEU C CD1   1 
ATOM   7413  C  CD2   . LEU K  3 262 ? 69.949  37.622  158.038 1.00 35.68 ? 262  LEU C CD2   1 
ATOM   7414  N  N     . ASP K  3 263 ? 71.060  42.159  156.978 1.00 20.77 ? 263  ASP C N     1 
ATOM   7415  C  CA    . ASP K  3 263 ? 70.244  43.363  156.901 1.00 22.92 ? 263  ASP C CA    1 
ATOM   7416  C  C     . ASP K  3 263 ? 69.784  43.587  155.450 1.00 24.92 ? 263  ASP C C     1 
ATOM   7417  O  O     . ASP K  3 263 ? 68.618  43.885  155.217 1.00 23.81 ? 263  ASP C O     1 
ATOM   7418  C  CB    . ASP K  3 263 ? 71.024  44.601  157.343 1.00 25.43 ? 263  ASP C CB    1 
ATOM   7419  C  CG    . ASP K  3 263 ? 71.075  44.773  158.869 1.00 29.55 ? 263  ASP C CG    1 
ATOM   7420  O  OD1   . ASP K  3 263 ? 70.404  44.016  159.598 1.00 29.96 ? 263  ASP C OD1   1 
ATOM   7421  O  OD2   . ASP K  3 263 ? 71.786  45.690  159.315 1.00 33.37 ? 263  ASP C OD2   1 
ATOM   7422  N  N     . LEU K  3 264 ? 70.705  43.431  154.497 1.00 21.68 ? 264  LEU C N     1 
ATOM   7423  C  CA    . LEU K  3 264 ? 70.378  43.642  153.076 1.00 20.80 ? 264  LEU C CA    1 
ATOM   7424  C  C     . LEU K  3 264 ? 69.371  42.601  152.597 1.00 19.84 ? 264  LEU C C     1 
ATOM   7425  O  O     . LEU K  3 264 ? 68.443  42.923  151.840 1.00 20.09 ? 264  LEU C O     1 
ATOM   7426  C  CB    . LEU K  3 264 ? 71.647  43.579  152.218 1.00 21.04 ? 264  LEU C CB    1 
ATOM   7427  C  CG    . LEU K  3 264 ? 71.500  43.932  150.723 1.00 19.75 ? 264  LEU C CG    1 
ATOM   7428  C  CD1   . LEU K  3 264 ? 70.754  45.216  150.531 1.00 19.85 ? 264  LEU C CD1   1 
ATOM   7429  C  CD2   . LEU K  3 264 ? 72.886  44.001  150.124 1.00 21.16 ? 264  LEU C CD2   1 
ATOM   7430  N  N     . PHE K  3 265 ? 69.576  41.357  153.012 1.00 19.40 ? 265  PHE C N     1 
ATOM   7431  C  CA    . PHE K  3 265 ? 68.649  40.265  152.693 1.00 19.30 ? 265  PHE C CA    1 
ATOM   7432  C  C     . PHE K  3 265 ? 67.232  40.681  153.112 1.00 20.32 ? 265  PHE C C     1 
ATOM   7433  O  O     . PHE K  3 265 ? 66.295  40.602  152.321 1.00 18.53 ? 265  PHE C O     1 
ATOM   7434  C  CB    . PHE K  3 265 ? 69.027  39.002  153.471 1.00 20.62 ? 265  PHE C CB    1 
ATOM   7435  C  CG    . PHE K  3 265 ? 68.065  37.874  153.296 1.00 21.32 ? 265  PHE C CG    1 
ATOM   7436  C  CD1   . PHE K  3 265 ? 68.212  36.957  152.244 1.00 17.98 ? 265  PHE C CD1   1 
ATOM   7437  C  CD2   . PHE K  3 265 ? 67.022  37.704  154.191 1.00 18.32 ? 265  PHE C CD2   1 
ATOM   7438  C  CE1   . PHE K  3 265 ? 67.325  35.883  152.105 1.00 19.93 ? 265  PHE C CE1   1 
ATOM   7439  C  CE2   . PHE K  3 265 ? 66.132  36.648  154.072 1.00 18.17 ? 265  PHE C CE2   1 
ATOM   7440  C  CZ    . PHE K  3 265 ? 66.277  35.722  153.025 1.00 19.34 ? 265  PHE C CZ    1 
ATOM   7441  N  N     . TYR K  3 266 ? 67.065  41.113  154.367 1.00 18.64 ? 266  TYR C N     1 
ATOM   7442  C  CA    . TYR K  3 266 ? 65.741  41.501  154.831 1.00 20.41 ? 266  TYR C CA    1 
ATOM   7443  C  C     . TYR K  3 266 ? 65.156  42.750  154.173 1.00 19.03 ? 266  TYR C C     1 
ATOM   7444  O  O     . TYR K  3 266 ? 63.941  42.850  154.020 1.00 22.49 ? 266  TYR C O     1 
ATOM   7445  C  CB    . TYR K  3 266 ? 65.712  41.595  156.369 1.00 22.26 ? 266  TYR C CB    1 
ATOM   7446  C  CG    . TYR K  3 266 ? 65.693  40.215  157.002 1.00 24.93 ? 266  TYR C CG    1 
ATOM   7447  C  CD1   . TYR K  3 266 ? 66.750  39.775  157.794 1.00 26.78 ? 266  TYR C CD1   1 
ATOM   7448  C  CD2   . TYR K  3 266 ? 64.630  39.331  156.772 1.00 24.38 ? 266  TYR C CD2   1 
ATOM   7449  C  CE1   . TYR K  3 266 ? 66.756  38.495  158.341 1.00 28.78 ? 266  TYR C CE1   1 
ATOM   7450  C  CE2   . TYR K  3 266 ? 64.631  38.039  157.314 1.00 27.95 ? 266  TYR C CE2   1 
ATOM   7451  C  CZ    . TYR K  3 266 ? 65.710  37.633  158.104 1.00 28.28 ? 266  TYR C CZ    1 
ATOM   7452  O  OH    . TYR K  3 266 ? 65.755  36.363  158.659 1.00 30.11 ? 266  TYR C OH    1 
ATOM   7453  N  N     . ILE K  3 267 ? 65.994  43.707  153.785 1.00 18.28 ? 267  ILE C N     1 
ATOM   7454  C  CA    . ILE K  3 267 ? 65.484  44.872  153.073 1.00 16.61 ? 267  ILE C CA    1 
ATOM   7455  C  C     . ILE K  3 267 ? 64.849  44.356  151.770 1.00 18.68 ? 267  ILE C C     1 
ATOM   7456  O  O     . ILE K  3 267 ? 63.744  44.764  151.400 1.00 19.15 ? 267  ILE C O     1 
ATOM   7457  C  CB    . ILE K  3 267 ? 66.624  45.866  152.730 1.00 20.31 ? 267  ILE C CB    1 
ATOM   7458  C  CG1   . ILE K  3 267 ? 67.032  46.647  153.993 1.00 22.69 ? 267  ILE C CG1   1 
ATOM   7459  C  CG2   . ILE K  3 267 ? 66.188  46.861  151.648 1.00 19.48 ? 267  ILE C CG2   1 
ATOM   7460  C  CD1   . ILE K  3 267 ? 68.282  47.488  153.760 1.00 27.94 ? 267  ILE C CD1   1 
ATOM   7461  N  N     . MET K  3 268 ? 65.540  43.457  151.072 1.00 17.98 ? 268  MET C N     1 
ATOM   7462  C  CA    . MET K  3 268 ? 64.981  42.956  149.822 1.00 18.14 ? 268  MET C CA    1 
ATOM   7463  C  C     . MET K  3 268 ? 63.755  42.083  149.999 1.00 18.05 ? 268  MET C C     1 
ATOM   7464  O  O     . MET K  3 268 ? 62.782  42.206  149.246 1.00 18.09 ? 268  MET C O     1 
ATOM   7465  C  CB    . MET K  3 268 ? 66.042  42.188  149.016 1.00 16.82 ? 268  MET C CB    1 
ATOM   7466  C  CG    . MET K  3 268 ? 67.196  43.055  148.544 1.00 15.06 ? 268  MET C CG    1 
ATOM   7467  S  SD    . MET K  3 268 ? 68.405  42.156  147.584 1.00 17.10 ? 268  MET C SD    1 
ATOM   7468  C  CE    . MET K  3 268 ? 69.209  41.119  148.840 1.00 15.32 ? 268  MET C CE    1 
ATOM   7469  N  N     . VAL K  3 269 ? 63.777  41.205  150.993 1.00 18.67 ? 269  VAL C N     1 
ATOM   7470  C  CA    . VAL K  3 269 ? 62.652  40.306  151.228 1.00 19.11 ? 269  VAL C CA    1 
ATOM   7471  C  C     . VAL K  3 269 ? 61.439  41.033  151.842 1.00 21.37 ? 269  VAL C C     1 
ATOM   7472  O  O     . VAL K  3 269 ? 60.309  40.892  151.359 1.00 21.08 ? 269  VAL C O     1 
ATOM   7473  C  CB    . VAL K  3 269 ? 63.084  39.120  152.114 1.00 19.51 ? 269  VAL C CB    1 
ATOM   7474  C  CG1   . VAL K  3 269 ? 61.875  38.258  152.466 1.00 20.79 ? 269  VAL C CG1   1 
ATOM   7475  C  CG2   . VAL K  3 269 ? 64.139  38.284  151.380 1.00 18.52 ? 269  VAL C CG2   1 
ATOM   7476  N  N     . ASN K  3 270 ? 61.654  41.822  152.891 1.00 20.05 ? 270  ASN C N     1 
ATOM   7477  C  CA    . ASN K  3 270 ? 60.529  42.541  153.488 1.00 22.84 ? 270  ASN C CA    1 
ATOM   7478  C  C     . ASN K  3 270 ? 60.036  43.593  152.508 1.00 20.56 ? 270  ASN C C     1 
ATOM   7479  O  O     . ASN K  3 270 ? 58.865  43.985  152.537 1.00 23.58 ? 270  ASN C O     1 
ATOM   7480  C  CB    . ASN K  3 270 ? 60.946  43.211  154.803 1.00 23.62 ? 270  ASN C CB    1 
ATOM   7481  C  CG    . ASN K  3 270 ? 61.296  42.201  155.873 1.00 28.10 ? 270  ASN C CG    1 
ATOM   7482  O  OD1   . ASN K  3 270 ? 60.956  41.027  155.761 1.00 28.15 ? 270  ASN C OD1   1 
ATOM   7483  N  ND2   . ASN K  3 270 ? 61.974  42.655  156.925 1.00 28.26 ? 270  ASN C ND2   1 
ATOM   7484  N  N     . GLY K  3 271 ? 60.943  44.040  151.635 1.00 20.46 ? 271  GLY C N     1 
ATOM   7485  C  CA    . GLY K  3 271 ? 60.621  45.041  150.640 1.00 17.53 ? 271  GLY C CA    1 
ATOM   7486  C  C     . GLY K  3 271 ? 60.016  44.504  149.343 1.00 17.12 ? 271  GLY C C     1 
ATOM   7487  O  O     . GLY K  3 271 ? 59.876  45.253  148.374 1.00 19.07 ? 271  GLY C O     1 
ATOM   7488  N  N     . LYS K  3 272 ? 59.675  43.225  149.347 1.00 18.24 ? 272  LYS C N     1 
ATOM   7489  C  CA    . LYS K  3 272 ? 59.060  42.566  148.193 1.00 18.02 ? 272  LYS C CA    1 
ATOM   7490  C  C     . LYS K  3 272 ? 59.855  42.705  146.899 1.00 20.53 ? 272  LYS C C     1 
ATOM   7491  O  O     . LYS K  3 272 ? 59.293  42.923  145.809 1.00 18.45 ? 272  LYS C O     1 
ATOM   7492  C  CB    . LYS K  3 272 ? 57.630  43.066  148.000 1.00 20.34 ? 272  LYS C CB    1 
ATOM   7493  C  CG    . LYS K  3 272 ? 56.752  42.861  149.239 1.00 27.59 ? 272  LYS C CG    1 
ATOM   7494  C  CD    . LYS K  3 272 ? 55.291  43.158  148.930 1.00 35.95 ? 272  LYS C CD    1 
ATOM   7495  C  CE    . LYS K  3 272 ? 55.100  44.592  148.469 1.00 38.99 ? 272  LYS C CE    1 
ATOM   7496  N  NZ    . LYS K  3 272 ? 53.673  44.903  148.199 1.00 40.97 ? 272  LYS C NZ    1 
ATOM   7497  N  N     . ARG K  3 273 ? 61.175  42.584  147.030 1.00 16.99 ? 273  ARG C N     1 
ATOM   7498  C  CA    . ARG K  3 273 ? 62.044  42.621  145.852 1.00 17.39 ? 273  ARG C CA    1 
ATOM   7499  C  C     . ARG K  3 273 ? 62.681  41.256  145.619 1.00 16.26 ? 273  ARG C C     1 
ATOM   7500  O  O     . ARG K  3 273 ? 63.229  40.983  144.546 1.00 15.85 ? 273  ARG C O     1 
ATOM   7501  C  CB    . ARG K  3 273 ? 63.157  43.654  146.005 1.00 12.96 ? 273  ARG C CB    1 
ATOM   7502  C  CG    . ARG K  3 273 ? 62.691  45.082  146.318 1.00 16.12 ? 273  ARG C CG    1 
ATOM   7503  C  CD    . ARG K  3 273 ? 61.515  45.546  145.472 1.00 17.20 ? 273  ARG C CD    1 
ATOM   7504  N  NE    . ARG K  3 273 ? 61.848  45.740  144.051 1.00 16.03 ? 273  ARG C NE    1 
ATOM   7505  C  CZ    . ARG K  3 273 ? 61.170  45.198  143.037 1.00 17.02 ? 273  ARG C CZ    1 
ATOM   7506  N  NH1   . ARG K  3 273 ? 60.131  44.405  143.276 1.00 15.83 ? 273  ARG C NH1   1 
ATOM   7507  N  NH2   . ARG K  3 273 ? 61.502  45.496  141.779 1.00 17.00 ? 273  ARG C NH2   1 
ATOM   7508  N  N     . LEU K  3 274 ? 62.596  40.379  146.618 1.00 15.69 ? 274  LEU C N     1 
ATOM   7509  C  CA    . LEU K  3 274 ? 63.223  39.071  146.519 1.00 13.34 ? 274  LEU C CA    1 
ATOM   7510  C  C     . LEU K  3 274 ? 62.343  38.017  147.185 1.00 15.27 ? 274  LEU C C     1 
ATOM   7511  O  O     . LEU K  3 274 ? 61.858  38.222  148.318 1.00 18.09 ? 274  LEU C O     1 
ATOM   7512  C  CB    . LEU K  3 274 ? 64.604  39.128  147.207 1.00 14.61 ? 274  LEU C CB    1 
ATOM   7513  C  CG    . LEU K  3 274 ? 65.451  37.857  147.210 1.00 14.33 ? 274  LEU C CG    1 
ATOM   7514  C  CD1   . LEU K  3 274 ? 65.848  37.510  145.770 1.00 15.83 ? 274  LEU C CD1   1 
ATOM   7515  C  CD2   . LEU K  3 274 ? 66.693  38.066  148.108 1.00 16.20 ? 274  LEU C CD2   1 
ATOM   7516  N  N     . LYS K  3 275 ? 62.133  36.908  146.484 1.00 12.41 ? 275  LYS C N     1 
ATOM   7517  C  CA    . LYS K  3 275 ? 61.313  35.806  146.989 1.00 11.98 ? 275  LYS C CA    1 
ATOM   7518  C  C     . LYS K  3 275 ? 62.019  34.480  146.726 1.00 15.01 ? 275  LYS C C     1 
ATOM   7519  O  O     . LYS K  3 275 ? 63.163  34.456  146.279 1.00 15.19 ? 275  LYS C O     1 
ATOM   7520  C  CB    . LYS K  3 275 ? 59.936  35.834  146.300 1.00 13.43 ? 275  LYS C CB    1 
ATOM   7521  C  CG    . LYS K  3 275 ? 59.123  37.095  146.582 1.00 13.41 ? 275  LYS C CG    1 
ATOM   7522  C  CD    . LYS K  3 275 ? 57.735  36.994  145.907 1.00 13.40 ? 275  LYS C CD    1 
ATOM   7523  C  CE    . LYS K  3 275 ? 56.926  38.256  146.121 1.00 15.09 ? 275  LYS C CE    1 
ATOM   7524  N  NZ    . LYS K  3 275 ? 55.472  38.074  145.658 1.00 15.95 ? 275  LYS C NZ    1 
ATOM   7525  N  N     . ASP K  3 276 ? 61.359  33.368  147.021 1.00 15.63 ? 276  ASP C N     1 
ATOM   7526  C  CA    . ASP K  3 276 ? 61.949  32.062  146.765 1.00 15.13 ? 276  ASP C CA    1 
ATOM   7527  C  C     . ASP K  3 276 ? 61.491  31.557  145.389 1.00 12.70 ? 276  ASP C C     1 
ATOM   7528  O  O     . ASP K  3 276 ? 60.432  31.942  144.866 1.00 13.98 ? 276  ASP C O     1 
ATOM   7529  C  CB    . ASP K  3 276 ? 61.485  31.040  147.837 1.00 15.15 ? 276  ASP C CB    1 
ATOM   7530  C  CG    . ASP K  3 276 ? 62.137  29.672  147.668 1.00 15.32 ? 276  ASP C CG    1 
ATOM   7531  O  OD1   . ASP K  3 276 ? 63.378  29.581  147.817 1.00 17.90 ? 276  ASP C OD1   1 
ATOM   7532  O  OD2   . ASP K  3 276 ? 61.432  28.683  147.383 1.00 17.15 ? 276  ASP C OD2   1 
ATOM   7533  N  N     . ILE K  3 277 ? 62.260  30.631  144.835 1.00 14.78 ? 277  ILE C N     1 
ATOM   7534  C  CA    . ILE K  3 277 ? 61.892  30.011  143.568 1.00 16.14 ? 277  ILE C CA    1 
ATOM   7535  C  C     . ILE K  3 277 ? 60.469  29.421  143.664 1.00 17.93 ? 277  ILE C C     1 
ATOM   7536  O  O     . ILE K  3 277 ? 59.706  29.478  142.703 1.00 15.91 ? 277  ILE C O     1 
ATOM   7537  C  CB    . ILE K  3 277 ? 62.929  28.895  143.200 1.00 18.37 ? 277  ILE C CB    1 
ATOM   7538  C  CG1   . ILE K  3 277 ? 62.528  28.172  141.913 1.00 19.17 ? 277  ILE C CG1   1 
ATOM   7539  C  CG2   . ILE K  3 277 ? 63.075  27.884  144.348 1.00 20.81 ? 277  ILE C CG2   1 
ATOM   7540  C  CD1   . ILE K  3 277 ? 62.536  29.063  140.704 1.00 18.93 ? 277  ILE C CD1   1 
ATOM   7541  N  N     . SER K  3 278 ? 60.085  28.886  144.832 1.00 16.05 ? 278  SER C N     1 
ATOM   7542  C  CA    . SER K  3 278 ? 58.744  28.293  144.958 1.00 16.47 ? 278  SER C CA    1 
ATOM   7543  C  C     . SER K  3 278 ? 57.582  29.301  144.889 1.00 15.45 ? 278  SER C C     1 
ATOM   7544  O  O     . SER K  3 278 ? 56.429  28.912  144.733 1.00 15.55 ? 278  SER C O     1 
ATOM   7545  C  CB    . SER K  3 278 ? 58.629  27.494  146.279 1.00 15.05 ? 278  SER C CB    1 
ATOM   7546  O  OG    . SER K  3 278 ? 58.714  28.358  147.382 1.00 15.42 ? 278  SER C OG    1 
ATOM   7547  N  N     . ASP K  3 279 ? 57.894  30.587  145.011 1.00 13.79 ? 279  ASP C N     1 
ATOM   7548  C  CA    . ASP K  3 279 ? 56.884  31.639  144.938 1.00 13.76 ? 279  ASP C CA    1 
ATOM   7549  C  C     . ASP K  3 279 ? 56.578  31.973  143.484 1.00 15.12 ? 279  ASP C C     1 
ATOM   7550  O  O     . ASP K  3 279 ? 55.511  32.497  143.187 1.00 15.52 ? 279  ASP C O     1 
ATOM   7551  C  CB    . ASP K  3 279 ? 57.389  32.930  145.599 1.00 14.12 ? 279  ASP C CB    1 
ATOM   7552  C  CG    . ASP K  3 279 ? 57.502  32.809  147.126 1.00 17.31 ? 279  ASP C CG    1 
ATOM   7553  O  OD1   . ASP K  3 279 ? 56.462  32.483  147.739 1.00 18.14 ? 279  ASP C OD1   1 
ATOM   7554  O  OD2   . ASP K  3 279 ? 58.616  33.019  147.679 1.00 14.98 ? 279  ASP C OD2   1 
ATOM   7555  N  N     . LEU K  3 280 ? 57.527  31.699  142.599 1.00 14.18 ? 280  LEU C N     1 
ATOM   7556  C  CA    . LEU K  3 280 ? 57.329  32.066  141.188 1.00 15.76 ? 280  LEU C CA    1 
ATOM   7557  C  C     . LEU K  3 280 ? 56.091  31.510  140.465 1.00 16.11 ? 280  LEU C C     1 
ATOM   7558  O  O     . LEU K  3 280 ? 55.359  32.286  139.856 1.00 14.60 ? 280  LEU C O     1 
ATOM   7559  C  CB    . LEU K  3 280 ? 58.603  31.768  140.377 1.00 14.59 ? 280  LEU C CB    1 
ATOM   7560  C  CG    . LEU K  3 280 ? 58.541  32.169  138.887 1.00 16.55 ? 280  LEU C CG    1 
ATOM   7561  C  CD1   . LEU K  3 280 ? 58.133  33.642  138.694 1.00 17.96 ? 280  LEU C CD1   1 
ATOM   7562  C  CD2   . LEU K  3 280 ? 59.922  31.890  138.274 1.00 15.61 ? 280  LEU C CD2   1 
ATOM   7563  N  N     . PRO K  3 281 ? 55.825  30.190  140.544 1.00 16.46 ? 281  PRO C N     1 
ATOM   7564  C  CA    . PRO K  3 281 ? 54.645  29.639  139.857 1.00 17.08 ? 281  PRO C CA    1 
ATOM   7565  C  C     . PRO K  3 281 ? 53.365  30.343  140.270 1.00 18.20 ? 281  PRO C C     1 
ATOM   7566  O  O     . PRO K  3 281 ? 52.536  30.704  139.432 1.00 14.56 ? 281  PRO C O     1 
ATOM   7567  C  CB    . PRO K  3 281 ? 54.653  28.169  140.275 1.00 16.76 ? 281  PRO C CB    1 
ATOM   7568  C  CG    . PRO K  3 281 ? 56.096  27.875  140.471 1.00 16.58 ? 281  PRO C CG    1 
ATOM   7569  C  CD    . PRO K  3 281 ? 56.583  29.114  141.210 1.00 17.47 ? 281  PRO C CD    1 
ATOM   7570  N  N     . LEU K  3 282 ? 53.173  30.529  141.583 1.00 15.45 ? 282  LEU C N     1 
ATOM   7571  C  CA    . LEU K  3 282 ? 51.982  31.232  142.031 1.00 17.83 ? 282  LEU C CA    1 
ATOM   7572  C  C     . LEU K  3 282 ? 51.965  32.704  141.610 1.00 16.11 ? 282  LEU C C     1 
ATOM   7573  O  O     . LEU K  3 282 ? 50.905  33.248  141.328 1.00 15.97 ? 282  LEU C O     1 
ATOM   7574  C  CB    . LEU K  3 282 ? 51.818  31.127  143.563 1.00 19.66 ? 282  LEU C CB    1 
ATOM   7575  C  CG    . LEU K  3 282 ? 51.037  29.884  144.006 1.00 18.71 ? 282  LEU C CG    1 
ATOM   7576  C  CD1   . LEU K  3 282 ? 51.209  29.684  145.518 1.00 16.89 ? 282  LEU C CD1   1 
ATOM   7577  C  CD2   . LEU K  3 282 ? 49.560  30.066  143.691 1.00 21.68 ? 282  LEU C CD2   1 
ATOM   7578  N  N     . ASP K  3 283 ? 53.128  33.360  141.600 1.00 14.68 ? 283  ASP C N     1 
ATOM   7579  C  CA    . ASP K  3 283 ? 53.180  34.766  141.206 1.00 13.67 ? 283  ASP C CA    1 
ATOM   7580  C  C     . ASP K  3 283 ? 52.842  34.893  139.722 1.00 14.46 ? 283  ASP C C     1 
ATOM   7581  O  O     . ASP K  3 283 ? 52.345  35.934  139.293 1.00 18.32 ? 283  ASP C O     1 
ATOM   7582  C  CB    . ASP K  3 283 ? 54.545  35.368  141.516 1.00 15.45 ? 283  ASP C CB    1 
ATOM   7583  C  CG    . ASP K  3 283 ? 54.652  35.798  142.966 1.00 15.74 ? 283  ASP C CG    1 
ATOM   7584  O  OD1   . ASP K  3 283 ? 53.635  35.647  143.704 1.00 16.76 ? 283  ASP C OD1   1 
ATOM   7585  O  OD2   . ASP K  3 283 ? 55.726  36.292  143.361 1.00 14.99 ? 283  ASP C OD2   1 
ATOM   7586  N  N     . LEU K  3 284 ? 53.047  33.818  138.965 1.00 14.83 ? 284  LEU C N     1 
ATOM   7587  C  CA    . LEU K  3 284 ? 52.698  33.836  137.533 1.00 17.00 ? 284  LEU C CA    1 
ATOM   7588  C  C     . LEU K  3 284 ? 51.193  33.638  137.334 1.00 18.57 ? 284  LEU C C     1 
ATOM   7589  O  O     . LEU K  3 284 ? 50.704  33.710  136.209 1.00 16.71 ? 284  LEU C O     1 
ATOM   7590  C  CB    . LEU K  3 284 ? 53.450  32.737  136.771 1.00 15.21 ? 284  LEU C CB    1 
ATOM   7591  C  CG    . LEU K  3 284 ? 54.965  32.938  136.672 1.00 15.68 ? 284  LEU C CG    1 
ATOM   7592  C  CD1   . LEU K  3 284 ? 55.614  31.725  136.008 1.00 19.30 ? 284  LEU C CD1   1 
ATOM   7593  C  CD2   . LEU K  3 284 ? 55.260  34.217  135.883 1.00 22.11 ? 284  LEU C CD2   1 
ATOM   7594  N  N     . ALA K  3 285 ? 50.453  33.390  138.413 1.00 17.76 ? 285  ALA C N     1 
ATOM   7595  C  CA    . ALA K  3 285 ? 49.001  33.198  138.298 1.00 16.76 ? 285  ALA C CA    1 
ATOM   7596  C  C     . ALA K  3 285 ? 48.166  34.434  138.647 1.00 20.54 ? 285  ALA C C     1 
ATOM   7597  O  O     . ALA K  3 285 ? 46.939  34.353  138.662 1.00 20.21 ? 285  ALA C O     1 
ATOM   7598  C  CB    . ALA K  3 285 ? 48.550  32.020  139.192 1.00 17.75 ? 285  ALA C CB    1 
ATOM   7599  N  N     . VAL K  3 286 ? 48.782  35.580  138.935 1.00 18.66 ? 286  VAL C N     1 
ATOM   7600  C  CA    . VAL K  3 286 ? 47.958  36.734  139.314 1.00 21.89 ? 286  VAL C CA    1 
ATOM   7601  C  C     . VAL K  3 286 ? 46.976  37.201  138.212 1.00 21.90 ? 286  VAL C C     1 
ATOM   7602  O  O     . VAL K  3 286 ? 45.860  37.713  138.545 1.00 18.88 ? 286  VAL C O     1 
ATOM   7603  C  CB    . VAL K  3 286 ? 48.821  37.934  139.763 1.00 23.89 ? 286  VAL C CB    1 
ATOM   7604  C  CG1   . VAL K  3 286 ? 49.667  37.561  140.971 1.00 19.36 ? 286  VAL C CG1   1 
ATOM   7605  C  CG2   . VAL K  3 286 ? 49.679  38.393  138.630 1.00 26.12 ? 286  VAL C CG2   1 
ATOM   7606  O  OXT   . VAL K  3 286 ? 47.344  37.067  137.015 1.00 21.96 ? 286  VAL C OXT   1 
ATOM   7607  N  N     . MET L  3 1   ? 99.731  64.530  111.856 1.00 51.19 ? 1    MET D N     1 
ATOM   7608  C  CA    . MET L  3 1   ? 99.581  65.920  111.353 1.00 50.08 ? 1    MET D CA    1 
ATOM   7609  C  C     . MET L  3 1   ? 99.982  66.903  112.420 1.00 48.55 ? 1    MET D C     1 
ATOM   7610  O  O     . MET L  3 1   ? 100.562 66.541  113.439 1.00 54.75 ? 1    MET D O     1 
ATOM   7611  C  CB    . MET L  3 1   ? 98.132  66.193  110.925 1.00 52.82 ? 1    MET D CB    1 
ATOM   7612  C  CG    . MET L  3 1   ? 97.746  65.496  109.632 1.00 55.96 ? 1    MET D CG    1 
ATOM   7613  S  SD    . MET L  3 1   ? 96.142  65.996  108.983 1.00 60.04 ? 1    MET D SD    1 
ATOM   7614  C  CE    . MET L  3 1   ? 95.335  64.390  108.794 1.00 60.04 ? 1    MET D CE    1 
ATOM   7615  N  N     . GLN L  3 2   ? 99.661  68.161  112.182 1.00 43.38 ? 2    GLN D N     1 
ATOM   7616  C  CA    . GLN L  3 2   ? 100.019 69.164  113.128 1.00 37.01 ? 2    GLN D CA    1 
ATOM   7617  C  C     . GLN L  3 2   ? 98.871  69.763  113.916 1.00 23.27 ? 2    GLN D C     1 
ATOM   7618  O  O     . GLN L  3 2   ? 99.158  70.368  114.939 1.00 30.37 ? 2    GLN D O     1 
ATOM   7619  C  CB    . GLN L  3 2   ? 100.815 70.297  112.464 1.00 42.15 ? 2    GLN D CB    1 
ATOM   7620  C  CG    . GLN L  3 2   ? 101.145 70.110  111.003 1.00 46.28 ? 2    GLN D CG    1 
ATOM   7621  C  CD    . GLN L  3 2   ? 99.928  69.782  110.152 1.00 50.94 ? 2    GLN D CD    1 
ATOM   7622  O  OE1   . GLN L  3 2   ? 99.714  68.626  109.766 1.00 56.28 ? 2    GLN D OE1   1 
ATOM   7623  N  NE2   . GLN L  3 2   ? 99.117  70.791  109.863 1.00 51.74 ? 2    GLN D NE2   1 
ATOM   7624  N  N     . PRO L  3 3   ? 97.576  69.629  113.482 1.00 21.80 ? 3    PRO D N     1 
ATOM   7625  C  CA    . PRO L  3 3   ? 96.568  70.268  114.354 1.00 18.86 ? 3    PRO D CA    1 
ATOM   7626  C  C     . PRO L  3 3   ? 96.739  69.687  115.753 1.00 18.27 ? 3    PRO D C     1 
ATOM   7627  O  O     . PRO L  3 3   ? 97.064  68.498  115.886 1.00 18.46 ? 3    PRO D O     1 
ATOM   7628  C  CB    . PRO L  3 3   ? 95.226  69.854  113.732 1.00 23.09 ? 3    PRO D CB    1 
ATOM   7629  C  CG    . PRO L  3 3   ? 95.557  69.595  112.300 1.00 29.51 ? 3    PRO D CG    1 
ATOM   7630  C  CD    . PRO L  3 3   ? 96.908  68.918  112.370 1.00 23.65 ? 3    PRO D CD    1 
ATOM   7631  N  N     . LEU L  3 4   ? 96.484  70.489  116.786 1.00 15.32 ? 4    LEU D N     1 
ATOM   7632  C  CA    . LEU L  3 4   ? 96.696  69.994  118.141 1.00 15.67 ? 4    LEU D CA    1 
ATOM   7633  C  C     . LEU L  3 4   ? 95.764  68.834  118.524 1.00 18.77 ? 4    LEU D C     1 
ATOM   7634  O  O     . LEU L  3 4   ? 96.175  67.948  119.267 1.00 16.75 ? 4    LEU D O     1 
ATOM   7635  C  CB    . LEU L  3 4   ? 96.574  71.130  119.180 1.00 18.23 ? 4    LEU D CB    1 
ATOM   7636  C  CG    . LEU L  3 4   ? 97.669  72.219  119.166 1.00 24.80 ? 4    LEU D CG    1 
ATOM   7637  C  CD1   . LEU L  3 4   ? 97.429  73.200  120.324 1.00 24.87 ? 4    LEU D CD1   1 
ATOM   7638  C  CD2   . LEU L  3 4   ? 99.051  71.588  119.297 1.00 31.12 ? 4    LEU D CD2   1 
ATOM   7639  N  N     . PHE L  3 5   ? 94.525  68.823  118.044 1.00 17.09 ? 5    PHE D N     1 
ATOM   7640  C  CA    . PHE L  3 5   ? 93.667  67.689  118.403 1.00 16.42 ? 5    PHE D CA    1 
ATOM   7641  C  C     . PHE L  3 5   ? 94.183  66.406  117.737 1.00 17.55 ? 5    PHE D C     1 
ATOM   7642  O  O     . PHE L  3 5   ? 93.993  65.312  118.244 1.00 14.72 ? 5    PHE D O     1 
ATOM   7643  C  CB    . PHE L  3 5   ? 92.202  67.940  118.023 1.00 16.06 ? 5    PHE D CB    1 
ATOM   7644  C  CG    . PHE L  3 5   ? 91.478  68.876  118.972 1.00 16.73 ? 5    PHE D CG    1 
ATOM   7645  C  CD1   . PHE L  3 5   ? 90.135  69.149  118.781 1.00 21.95 ? 5    PHE D CD1   1 
ATOM   7646  C  CD2   . PHE L  3 5   ? 92.138  69.459  120.059 1.00 20.14 ? 5    PHE D CD2   1 
ATOM   7647  C  CE1   . PHE L  3 5   ? 89.440  70.001  119.662 1.00 24.65 ? 5    PHE D CE1   1 
ATOM   7648  C  CE2   . PHE L  3 5   ? 91.448  70.311  120.949 1.00 19.21 ? 5    PHE D CE2   1 
ATOM   7649  C  CZ    . PHE L  3 5   ? 90.099  70.574  120.740 1.00 17.54 ? 5    PHE D CZ    1 
ATOM   7650  N  N     . THR L  3 6   ? 94.825  66.540  116.584 1.00 15.22 ? 6    THR D N     1 
ATOM   7651  C  CA    . THR L  3 6   ? 95.389  65.377  115.901 1.00 16.63 ? 6    THR D CA    1 
ATOM   7652  C  C     . THR L  3 6   ? 96.598  64.894  116.715 1.00 17.20 ? 6    THR D C     1 
ATOM   7653  O  O     . THR L  3 6   ? 96.790  63.681  116.906 1.00 16.29 ? 6    THR D O     1 
ATOM   7654  C  CB    . THR L  3 6   ? 95.815  65.772  114.469 1.00 17.32 ? 6    THR D CB    1 
ATOM   7655  O  OG1   . THR L  3 6   ? 94.649  66.231  113.769 1.00 18.42 ? 6    THR D OG1   1 
ATOM   7656  C  CG2   . THR L  3 6   ? 96.461  64.588  113.721 1.00 22.15 ? 6    THR D CG2   1 
ATOM   7657  N  N     . GLN L  3 7   ? 97.392  65.836  117.225 1.00 16.24 ? 7    GLN D N     1 
ATOM   7658  C  CA    . GLN L  3 7   ? 98.559  65.472  118.029 1.00 15.12 ? 7    GLN D CA    1 
ATOM   7659  C  C     . GLN L  3 7   ? 98.089  64.821  119.325 1.00 17.37 ? 7    GLN D C     1 
ATOM   7660  O  O     . GLN L  3 7   ? 98.678  63.832  119.778 1.00 19.01 ? 7    GLN D O     1 
ATOM   7661  C  CB    . GLN L  3 7   ? 99.385  66.711  118.363 1.00 18.31 ? 7    GLN D CB    1 
ATOM   7662  C  CG    . GLN L  3 7   ? 100.143 67.282  117.174 1.00 21.95 ? 7    GLN D CG    1 
ATOM   7663  C  CD    . GLN L  3 7   ? 100.984 68.484  117.573 1.00 28.53 ? 7    GLN D CD    1 
ATOM   7664  O  OE1   . GLN L  3 7   ? 101.743 68.434  118.552 1.00 32.25 ? 7    GLN D OE1   1 
ATOM   7665  N  NE2   . GLN L  3 7   ? 100.852 69.574  116.821 1.00 28.05 ? 7    GLN D NE2   1 
ATOM   7666  N  N     . GLU L  3 8   ? 97.034  65.384  119.919 1.00 17.36 ? 8    GLU D N     1 
ATOM   7667  C  CA    . GLU L  3 8   ? 96.518  64.851  121.189 1.00 17.18 ? 8    GLU D CA    1 
ATOM   7668  C  C     . GLU L  3 8   ? 95.935  63.452  120.997 1.00 17.16 ? 8    GLU D C     1 
ATOM   7669  O  O     . GLU L  3 8   ? 96.062  62.597  121.886 1.00 18.28 ? 8    GLU D O     1 
ATOM   7670  C  CB    . GLU L  3 8   ? 95.454  65.782  121.782 1.00 19.05 ? 8    GLU D CB    1 
ATOM   7671  C  CG    . GLU L  3 8   ? 95.997  67.086  122.370 1.00 27.89 ? 8    GLU D CG    1 
ATOM   7672  C  CD    . GLU L  3 8   ? 96.869  66.872  123.606 1.00 37.14 ? 8    GLU D CD    1 
ATOM   7673  O  OE1   . GLU L  3 8   ? 96.757  65.803  124.254 1.00 41.82 ? 8    GLU D OE1   1 
ATOM   7674  O  OE2   . GLU L  3 8   ? 97.663  67.783  123.940 1.00 43.65 ? 8    GLU D OE2   1 
ATOM   7675  N  N     . ARG L  3 9   ? 95.284  63.219  119.856 1.00 14.85 ? 9    ARG D N     1 
ATOM   7676  C  CA    . ARG L  3 9   ? 94.739  61.903  119.545 1.00 15.94 ? 9    ARG D CA    1 
ATOM   7677  C  C     . ARG L  3 9   ? 95.893  60.902  119.440 1.00 14.32 ? 9    ARG D C     1 
ATOM   7678  O  O     . ARG L  3 9   ? 95.805  59.791  119.952 1.00 16.69 ? 9    ARG D O     1 
ATOM   7679  C  CB    . ARG L  3 9   ? 93.959  61.963  118.234 1.00 17.56 ? 9    ARG D CB    1 
ATOM   7680  C  CG    . ARG L  3 9   ? 93.345  60.629  117.786 1.00 15.40 ? 9    ARG D CG    1 
ATOM   7681  C  CD    . ARG L  3 9   ? 92.612  60.857  116.465 1.00 16.65 ? 9    ARG D CD    1 
ATOM   7682  N  NE    . ARG L  3 9   ? 91.737  59.746  116.068 1.00 14.22 ? 9    ARG D NE    1 
ATOM   7683  C  CZ    . ARG L  3 9   ? 92.114  58.685  115.362 1.00 16.84 ? 9    ARG D CZ    1 
ATOM   7684  N  NH1   . ARG L  3 9   ? 93.390  58.560  114.948 1.00 16.96 ? 9    ARG D NH1   1 
ATOM   7685  N  NH2   . ARG L  3 9   ? 91.208  57.759  115.059 1.00 12.68 ? 9    ARG D NH2   1 
ATOM   7686  N  N     . ARG L  3 10  ? 97.005  61.311  118.831 1.00 14.33 ? 10   ARG D N     1 
ATOM   7687  C  CA    . ARG L  3 10  ? 98.155  60.419  118.701 1.00 13.79 ? 10   ARG D CA    1 
ATOM   7688  C  C     . ARG L  3 10  ? 98.790  60.173  120.063 1.00 15.48 ? 10   ARG D C     1 
ATOM   7689  O  O     . ARG L  3 10  ? 99.234  59.058  120.336 1.00 16.85 ? 10   ARG D O     1 
ATOM   7690  C  CB    . ARG L  3 10  ? 99.192  61.003  117.730 1.00 16.89 ? 10   ARG D CB    1 
ATOM   7691  C  CG    . ARG L  3 10  ? 100.465 60.139  117.614 1.00 18.67 ? 10   ARG D CG    1 
ATOM   7692  C  CD    . ARG L  3 10  ? 100.166 58.735  117.105 1.00 18.19 ? 10   ARG D CD    1 
ATOM   7693  N  NE    . ARG L  3 10  ? 101.363 57.882  117.174 1.00 17.06 ? 10   ARG D NE    1 
ATOM   7694  C  CZ    . ARG L  3 10  ? 101.367 56.567  116.966 1.00 18.00 ? 10   ARG D CZ    1 
ATOM   7695  N  NH1   . ARG L  3 10  ? 100.237 55.923  116.662 1.00 17.87 ? 10   ARG D NH1   1 
ATOM   7696  N  NH2   . ARG L  3 10  ? 102.499 55.870  117.108 1.00 18.42 ? 10   ARG D NH2   1 
ATOM   7697  N  N     . ILE L  3 11  ? 98.857  61.214  120.903 1.00 15.05 ? 11   ILE D N     1 
ATOM   7698  C  CA    . ILE L  3 11  ? 99.399  61.063  122.243 1.00 15.48 ? 11   ILE D CA    1 
ATOM   7699  C  C     . ILE L  3 11  ? 98.560  60.026  123.010 1.00 18.25 ? 11   ILE D C     1 
ATOM   7700  O  O     . ILE L  3 11  ? 99.101  59.195  123.753 1.00 16.90 ? 11   ILE D O     1 
ATOM   7701  C  CB    . ILE L  3 11  ? 99.424  62.418  122.970 1.00 17.08 ? 11   ILE D CB    1 
ATOM   7702  C  CG1   . ILE L  3 11  ? 100.576 63.264  122.407 1.00 16.78 ? 11   ILE D CG1   1 
ATOM   7703  C  CG2   . ILE L  3 11  ? 99.580  62.201  124.470 1.00 17.49 ? 11   ILE D CG2   1 
ATOM   7704  C  CD1   . ILE L  3 11  ? 100.547 64.730  122.863 1.00 19.20 ? 11   ILE D CD1   1 
ATOM   7705  N  N     . PHE L  3 12  ? 97.248  60.077  122.819 1.00 14.95 ? 12   PHE D N     1 
ATOM   7706  C  CA    . PHE L  3 12  ? 96.306  59.114  123.441 1.00 16.37 ? 12   PHE D CA    1 
ATOM   7707  C  C     . PHE L  3 12  ? 96.653  57.673  122.978 1.00 17.16 ? 12   PHE D C     1 
ATOM   7708  O  O     . PHE L  3 12  ? 96.817  56.744  123.793 1.00 16.82 ? 12   PHE D O     1 
ATOM   7709  C  CB    . PHE L  3 12  ? 94.896  59.561  123.007 1.00 15.29 ? 12   PHE D CB    1 
ATOM   7710  C  CG    . PHE L  3 12  ? 93.795  58.549  123.239 1.00 15.70 ? 12   PHE D CG    1 
ATOM   7711  C  CD1   . PHE L  3 12  ? 93.267  58.344  124.501 1.00 15.16 ? 12   PHE D CD1   1 
ATOM   7712  C  CD2   . PHE L  3 12  ? 93.243  57.863  122.158 1.00 16.52 ? 12   PHE D CD2   1 
ATOM   7713  C  CE1   . PHE L  3 12  ? 92.184  57.457  124.692 1.00 16.84 ? 12   PHE D CE1   1 
ATOM   7714  C  CE2   . PHE L  3 12  ? 92.172  56.981  122.323 1.00 16.73 ? 12   PHE D CE2   1 
ATOM   7715  C  CZ    . PHE L  3 12  ? 91.638  56.777  123.612 1.00 16.68 ? 12   PHE D CZ    1 
ATOM   7716  N  N     . HIS L  3 13  ? 96.778  57.470  121.668 1.00 16.22 ? 13   HIS D N     1 
ATOM   7717  C  CA    . HIS L  3 13  ? 97.140  56.144  121.176 1.00 13.94 ? 13   HIS D CA    1 
ATOM   7718  C  C     . HIS L  3 13  ? 98.502  55.714  121.688 1.00 16.14 ? 13   HIS D C     1 
ATOM   7719  O  O     . HIS L  3 13  ? 98.702  54.545  122.055 1.00 17.36 ? 13   HIS D O     1 
ATOM   7720  C  CB    . HIS L  3 13  ? 97.194  56.143  119.650 1.00 15.34 ? 13   HIS D CB    1 
ATOM   7721  C  CG    . HIS L  3 13  ? 95.844  56.190  119.016 1.00 15.00 ? 13   HIS D CG    1 
ATOM   7722  N  ND1   . HIS L  3 13  ? 95.657  56.498  117.686 1.00 19.79 ? 13   HIS D ND1   1 
ATOM   7723  C  CD2   . HIS L  3 13  ? 94.615  55.927  119.522 1.00 15.88 ? 13   HIS D CD2   1 
ATOM   7724  C  CE1   . HIS L  3 13  ? 94.368  56.420  117.398 1.00 20.78 ? 13   HIS D CE1   1 
ATOM   7725  N  NE2   . HIS L  3 13  ? 93.714  56.075  118.495 1.00 15.93 ? 13   HIS D NE2   1 
ATOM   7726  N  N     . LYS L  3 14  ? 99.450  56.656  121.711 1.00 15.18 ? 14   LYS D N     1 
ATOM   7727  C  CA    . LYS L  3 14  ? 100.806 56.323  122.140 1.00 16.74 ? 14   LYS D CA    1 
ATOM   7728  C  C     . LYS L  3 14  ? 100.857 55.920  123.610 1.00 16.14 ? 14   LYS D C     1 
ATOM   7729  O  O     . LYS L  3 14  ? 101.667 55.080  123.987 1.00 19.15 ? 14   LYS D O     1 
ATOM   7730  C  CB    . LYS L  3 14  ? 101.739 57.503  121.823 1.00 19.48 ? 14   LYS D CB    1 
ATOM   7731  C  CG    . LYS L  3 14  ? 103.232 57.226  121.903 1.00 23.75 ? 14   LYS D CG    1 
ATOM   7732  C  CD    . LYS L  3 14  ? 103.698 56.256  120.806 1.00 24.51 ? 14   LYS D CD    1 
ATOM   7733  C  CE    . LYS L  3 14  ? 105.214 56.359  120.643 1.00 28.18 ? 14   LYS D CE    1 
ATOM   7734  N  NZ    . LYS L  3 14  ? 105.920 55.266  121.308 1.00 30.21 ? 14   LYS D NZ    1 
ATOM   7735  N  N     . LYS L  3 15  ? 99.998  56.500  124.446 1.00 17.55 ? 15   LYS D N     1 
ATOM   7736  C  CA    . LYS L  3 15  ? 99.974  56.098  125.848 1.00 16.03 ? 15   LYS D CA    1 
ATOM   7737  C  C     . LYS L  3 15  ? 99.504  54.652  125.942 1.00 17.15 ? 15   LYS D C     1 
ATOM   7738  O  O     . LYS L  3 15  ? 99.994  53.874  126.773 1.00 18.23 ? 15   LYS D O     1 
ATOM   7739  C  CB    . LYS L  3 15  ? 99.028  56.979  126.664 1.00 17.74 ? 15   LYS D CB    1 
ATOM   7740  C  CG    . LYS L  3 15  ? 99.661  58.296  127.054 1.00 16.85 ? 15   LYS D CG    1 
ATOM   7741  C  CD    . LYS L  3 15  ? 98.664  59.196  127.744 1.00 15.87 ? 15   LYS D CD    1 
ATOM   7742  C  CE    . LYS L  3 15  ? 99.299  60.515  128.040 1.00 19.06 ? 15   LYS D CE    1 
ATOM   7743  N  NZ    . LYS L  3 15  ? 98.277  61.434  128.623 1.00 23.55 ? 15   LYS D NZ    1 
ATOM   7744  N  N     . LEU L  3 16  ? 98.522  54.287  125.118 1.00 16.47 ? 16   LEU D N     1 
ATOM   7745  C  CA    . LEU L  3 16  ? 98.018  52.914  125.124 1.00 15.68 ? 16   LEU D CA    1 
ATOM   7746  C  C     . LEU L  3 16  ? 99.117  51.955  124.662 1.00 17.87 ? 16   LEU D C     1 
ATOM   7747  O  O     . LEU L  3 16  ? 99.294  50.881  125.237 1.00 19.62 ? 16   LEU D O     1 
ATOM   7748  C  CB    . LEU L  3 16  ? 96.796  52.797  124.186 1.00 17.15 ? 16   LEU D CB    1 
ATOM   7749  C  CG    . LEU L  3 16  ? 95.565  53.580  124.663 1.00 17.38 ? 16   LEU D CG    1 
ATOM   7750  C  CD1   . LEU L  3 16  ? 94.491  53.562  123.586 1.00 15.26 ? 16   LEU D CD1   1 
ATOM   7751  C  CD2   . LEU L  3 16  ? 94.999  52.935  125.943 1.00 20.78 ? 16   LEU D CD2   1 
ATOM   7752  N  N     . LEU L  3 17  ? 99.848  52.337  123.614 1.00 16.62 ? 17   LEU D N     1 
ATOM   7753  C  CA    . LEU L  3 17  ? 100.921 51.496  123.103 1.00 17.60 ? 17   LEU D CA    1 
ATOM   7754  C  C     . LEU L  3 17  ? 102.096 51.418  124.082 1.00 19.15 ? 17   LEU D C     1 
ATOM   7755  O  O     . LEU L  3 17  ? 102.595 50.326  124.404 1.00 19.67 ? 17   LEU D O     1 
ATOM   7756  C  CB    . LEU L  3 17  ? 101.412 52.047  121.752 1.00 18.37 ? 17   LEU D CB    1 
ATOM   7757  C  CG    . LEU L  3 17  ? 100.401 52.099  120.603 1.00 20.13 ? 17   LEU D CG    1 
ATOM   7758  C  CD1   . LEU L  3 17  ? 100.941 53.003  119.496 1.00 21.42 ? 17   LEU D CD1   1 
ATOM   7759  C  CD2   . LEU L  3 17  ? 100.125 50.689  120.060 1.00 18.64 ? 17   LEU D CD2   1 
ATOM   7760  N  N     . ASP L  3 18  ? 102.526 52.564  124.588 1.00 19.34 ? 18   ASP D N     1 
ATOM   7761  C  CA    . ASP L  3 18  ? 103.685 52.565  125.476 1.00 20.92 ? 18   ASP D CA    1 
ATOM   7762  C  C     . ASP L  3 18  ? 103.457 51.832  126.779 1.00 21.63 ? 18   ASP D C     1 
ATOM   7763  O  O     . ASP L  3 18  ? 104.416 51.338  127.381 1.00 23.18 ? 18   ASP D O     1 
ATOM   7764  C  CB    . ASP L  3 18  ? 104.169 53.996  125.737 1.00 20.18 ? 18   ASP D CB    1 
ATOM   7765  C  CG    . ASP L  3 18  ? 104.782 54.648  124.482 1.00 22.97 ? 18   ASP D CG    1 
ATOM   7766  O  OD1   . ASP L  3 18  ? 105.131 53.926  123.513 1.00 23.80 ? 18   ASP D OD1   1 
ATOM   7767  O  OD2   . ASP L  3 18  ? 104.917 55.890  124.473 1.00 24.15 ? 18   ASP D OD2   1 
ATOM   7768  N  N     . GLY L  3 19  ? 102.209 51.763  127.240 1.00 19.48 ? 19   GLY D N     1 
ATOM   7769  C  CA    . GLY L  3 19  ? 101.959 51.039  128.475 1.00 18.17 ? 19   GLY D CA    1 
ATOM   7770  C  C     . GLY L  3 19  ? 101.589 49.590  128.222 1.00 18.53 ? 19   GLY D C     1 
ATOM   7771  O  O     . GLY L  3 19  ? 101.210 48.878  129.152 1.00 20.57 ? 19   GLY D O     1 
ATOM   7772  N  N     . ASN L  3 20  ? 101.715 49.149  126.973 1.00 18.01 ? 20   ASN D N     1 
ATOM   7773  C  CA    . ASN L  3 20  ? 101.374 47.788  126.574 1.00 18.87 ? 20   ASN D CA    1 
ATOM   7774  C  C     . ASN L  3 20  ? 99.885  47.454  126.781 1.00 19.02 ? 20   ASN D C     1 
ATOM   7775  O  O     . ASN L  3 20  ? 99.497  46.278  126.824 1.00 19.17 ? 20   ASN D O     1 
ATOM   7776  C  CB    . ASN L  3 20  ? 102.258 46.768  127.321 1.00 22.81 ? 20   ASN D CB    1 
ATOM   7777  C  CG    . ASN L  3 20  ? 103.689 46.756  126.810 1.00 30.80 ? 20   ASN D CG    1 
ATOM   7778  O  OD1   . ASN L  3 20  ? 104.529 46.000  127.301 1.00 37.18 ? 20   ASN D OD1   1 
ATOM   7779  N  ND2   . ASN L  3 20  ? 103.972 47.589  125.822 1.00 27.57 ? 20   ASN D ND2   1 
ATOM   7780  N  N     . ILE L  3 21  ? 99.047  48.486  126.877 1.00 17.69 ? 21   ILE D N     1 
ATOM   7781  C  CA    . ILE L  3 21  ? 97.600  48.281  127.031 1.00 14.93 ? 21   ILE D CA    1 
ATOM   7782  C  C     . ILE L  3 21  ? 97.140  47.745  125.683 1.00 16.71 ? 21   ILE D C     1 
ATOM   7783  O  O     . ILE L  3 21  ? 96.354  46.793  125.613 1.00 17.41 ? 21   ILE D O     1 
ATOM   7784  C  CB    . ILE L  3 21  ? 96.850  49.601  127.356 1.00 17.16 ? 21   ILE D CB    1 
ATOM   7785  C  CG1   . ILE L  3 21  ? 97.471  50.296  128.577 1.00 24.40 ? 21   ILE D CG1   1 
ATOM   7786  C  CG2   . ILE L  3 21  ? 95.368  49.306  127.593 1.00 17.39 ? 21   ILE D CG2   1 
ATOM   7787  C  CD1   . ILE L  3 21  ? 97.645  49.403  129.745 1.00 28.16 ? 21   ILE D CD1   1 
ATOM   7788  N  N     . LEU L  3 22  ? 97.598  48.398  124.610 1.00 16.19 ? 22   LEU D N     1 
ATOM   7789  C  CA    . LEU L  3 22  ? 97.317  47.943  123.259 1.00 16.36 ? 22   LEU D CA    1 
ATOM   7790  C  C     . LEU L  3 22  ? 98.636  47.346  122.767 1.00 17.63 ? 22   LEU D C     1 
ATOM   7791  O  O     . LEU L  3 22  ? 99.608  48.079  122.571 1.00 18.35 ? 22   LEU D O     1 
ATOM   7792  C  CB    . LEU L  3 22  ? 96.930  49.097  122.324 1.00 14.96 ? 22   LEU D CB    1 
ATOM   7793  C  CG    . LEU L  3 22  ? 96.567  48.640  120.898 1.00 16.73 ? 22   LEU D CG    1 
ATOM   7794  C  CD1   . LEU L  3 22  ? 95.280  47.809  120.898 1.00 17.02 ? 22   LEU D CD1   1 
ATOM   7795  C  CD2   . LEU L  3 22  ? 96.390  49.865  120.014 1.00 17.49 ? 22   LEU D CD2   1 
ATOM   7796  N  N     . ALA L  3 23  ? 98.651  46.031  122.553 1.00 16.82 ? 23   ALA D N     1 
ATOM   7797  C  CA    . ALA L  3 23  ? 99.838  45.322  122.089 1.00 17.39 ? 23   ALA D CA    1 
ATOM   7798  C  C     . ALA L  3 23  ? 99.356  44.032  121.416 1.00 15.86 ? 23   ALA D C     1 
ATOM   7799  O  O     . ALA L  3 23  ? 98.155  43.756  121.352 1.00 17.91 ? 23   ALA D O     1 
ATOM   7800  C  CB    . ALA L  3 23  ? 100.764 45.001  123.266 1.00 18.79 ? 23   ALA D CB    1 
ATOM   7801  N  N     . THR L  3 24  ? 100.295 43.240  120.914 1.00 17.13 ? 24   THR D N     1 
ATOM   7802  C  CA    . THR L  3 24  ? 99.950  41.984  120.246 1.00 19.15 ? 24   THR D CA    1 
ATOM   7803  C  C     . THR L  3 24  ? 100.660 40.820  120.974 1.00 20.10 ? 24   THR D C     1 
ATOM   7804  O  O     . THR L  3 24  ? 101.852 40.924  121.282 1.00 19.27 ? 24   THR D O     1 
ATOM   7805  C  CB    . THR L  3 24  ? 100.436 41.984  118.766 1.00 18.69 ? 24   THR D CB    1 
ATOM   7806  O  OG1   . THR L  3 24  ? 99.926  43.130  118.069 1.00 19.44 ? 24   THR D OG1   1 
ATOM   7807  C  CG2   . THR L  3 24  ? 99.954  40.734  118.047 1.00 18.42 ? 24   THR D CG2   1 
ATOM   7808  N  N     . ASN L  3 25  ? 99.960  39.723  121.265 1.00 17.40 ? 25   ASN D N     1 
ATOM   7809  C  CA    . ASN L  3 25  ? 100.667 38.626  121.936 1.00 18.49 ? 25   ASN D CA    1 
ATOM   7810  C  C     . ASN L  3 25  ? 101.381 37.738  120.904 1.00 22.29 ? 25   ASN D C     1 
ATOM   7811  O  O     . ASN L  3 25  ? 101.303 37.993  119.691 1.00 18.43 ? 25   ASN D O     1 
ATOM   7812  C  CB    . ASN L  3 25  ? 99.730  37.802  122.860 1.00 18.96 ? 25   ASN D CB    1 
ATOM   7813  C  CG    . ASN L  3 25  ? 98.721  36.924  122.102 1.00 16.40 ? 25   ASN D CG    1 
ATOM   7814  O  OD1   . ASN L  3 25  ? 98.827  36.699  120.898 1.00 19.90 ? 25   ASN D OD1   1 
ATOM   7815  N  ND2   . ASN L  3 25  ? 97.736  36.411  122.838 1.00 22.32 ? 25   ASN D ND2   1 
ATOM   7816  N  N     . ASN L  3 26  ? 102.086 36.717  121.382 1.00 23.62 ? 26   ASN D N     1 
ATOM   7817  C  CA    . ASN L  3 26  ? 102.841 35.859  120.478 1.00 25.40 ? 26   ASN D CA    1 
ATOM   7818  C  C     . ASN L  3 26  ? 102.010 34.915  119.613 1.00 26.87 ? 26   ASN D C     1 
ATOM   7819  O  O     . ASN L  3 26  ? 102.572 34.121  118.853 1.00 26.35 ? 26   ASN D O     1 
ATOM   7820  C  CB    . ASN L  3 26  ? 103.914 35.067  121.237 1.00 30.19 ? 26   ASN D CB    1 
ATOM   7821  C  CG    . ASN L  3 26  ? 103.333 34.150  122.266 1.00 35.62 ? 26   ASN D CG    1 
ATOM   7822  O  OD1   . ASN L  3 26  ? 102.201 33.685  122.131 1.00 40.63 ? 26   ASN D OD1   1 
ATOM   7823  N  ND2   . ASN L  3 26  ? 104.108 33.870  123.311 1.00 40.84 ? 26   ASN D ND2   1 
ATOM   7824  N  N     . ARG L  3 27  ? 100.682 34.983  119.731 1.00 22.64 ? 27   ARG D N     1 
ATOM   7825  C  CA    . ARG L  3 27  ? 99.804  34.188  118.889 1.00 22.55 ? 27   ARG D CA    1 
ATOM   7826  C  C     . ARG L  3 27  ? 99.169  35.133  117.853 1.00 22.03 ? 27   ARG D C     1 
ATOM   7827  O  O     . ARG L  3 27  ? 98.307  34.731  117.070 1.00 24.29 ? 27   ARG D O     1 
ATOM   7828  C  CB    . ARG L  3 27  ? 98.713  33.503  119.721 1.00 29.26 ? 27   ARG D CB    1 
ATOM   7829  C  CG    . ARG L  3 27  ? 99.130  32.156  120.305 1.00 35.16 ? 27   ARG D CG    1 
ATOM   7830  C  CD    . ARG L  3 27  ? 99.802  32.313  121.640 1.00 41.53 ? 27   ARG D CD    1 
ATOM   7831  N  NE    . ARG L  3 27  ? 98.846  32.629  122.704 1.00 48.12 ? 27   ARG D NE    1 
ATOM   7832  C  CZ    . ARG L  3 27  ? 99.166  33.246  123.838 1.00 48.98 ? 27   ARG D CZ    1 
ATOM   7833  N  NH1   . ARG L  3 27  ? 100.420 33.625  124.061 1.00 48.10 ? 27   ARG D NH1   1 
ATOM   7834  N  NH2   . ARG L  3 27  ? 98.233  33.476  124.751 1.00 52.67 ? 27   ARG D NH2   1 
ATOM   7835  N  N     . GLY L  3 28  ? 99.591  36.401  117.875 1.00 19.87 ? 28   GLY D N     1 
ATOM   7836  C  CA    . GLY L  3 28  ? 99.066  37.373  116.929 1.00 21.36 ? 28   GLY D CA    1 
ATOM   7837  C  C     . GLY L  3 28  ? 97.788  38.092  117.362 1.00 20.05 ? 28   GLY D C     1 
ATOM   7838  O  O     . GLY L  3 28  ? 97.239  38.896  116.609 1.00 18.56 ? 28   GLY D O     1 
ATOM   7839  N  N     . VAL L  3 29  ? 97.315  37.812  118.570 1.00 19.96 ? 29   VAL D N     1 
ATOM   7840  C  CA    . VAL L  3 29  ? 96.078  38.446  119.043 1.00 18.02 ? 29   VAL D CA    1 
ATOM   7841  C  C     . VAL L  3 29  ? 96.345  39.825  119.648 1.00 16.22 ? 29   VAL D C     1 
ATOM   7842  O  O     . VAL L  3 29  ? 97.090  39.946  120.621 1.00 16.55 ? 29   VAL D O     1 
ATOM   7843  C  CB    . VAL L  3 29  ? 95.380  37.583  120.138 1.00 16.12 ? 29   VAL D CB    1 
ATOM   7844  C  CG1   . VAL L  3 29  ? 94.006  38.170  120.461 1.00 17.40 ? 29   VAL D CG1   1 
ATOM   7845  C  CG2   . VAL L  3 29  ? 95.216  36.137  119.675 1.00 19.40 ? 29   VAL D CG2   1 
ATOM   7846  N  N     . VAL L  3 30  ? 95.709  40.854  119.082 1.00 16.83 ? 30   VAL D N     1 
ATOM   7847  C  CA    . VAL L  3 30  ? 95.844  42.217  119.599 1.00 16.52 ? 30   VAL D CA    1 
ATOM   7848  C  C     . VAL L  3 30  ? 95.003  42.270  120.876 1.00 14.48 ? 30   VAL D C     1 
ATOM   7849  O  O     . VAL L  3 30  ? 93.936  41.647  120.960 1.00 14.42 ? 30   VAL D O     1 
ATOM   7850  C  CB    . VAL L  3 30  ? 95.413  43.240  118.520 1.00 18.32 ? 30   VAL D CB    1 
ATOM   7851  C  CG1   . VAL L  3 30  ? 95.451  44.658  119.085 1.00 19.15 ? 30   VAL D CG1   1 
ATOM   7852  C  CG2   . VAL L  3 30  ? 96.398  43.156  117.317 1.00 18.11 ? 30   VAL D CG2   1 
ATOM   7853  N  N     . SER L  3 31  ? 95.489  43.024  121.867 1.00 16.56 ? 31   SER D N     1 
ATOM   7854  C  CA    . SER L  3 31  ? 94.881  43.068  123.195 1.00 16.40 ? 31   SER D CA    1 
ATOM   7855  C  C     . SER L  3 31  ? 93.481  43.649  123.369 1.00 17.72 ? 31   SER D C     1 
ATOM   7856  O  O     . SER L  3 31  ? 92.927  43.569  124.466 1.00 17.22 ? 31   SER D O     1 
ATOM   7857  C  CB    . SER L  3 31  ? 95.859  43.727  124.161 1.00 17.33 ? 31   SER D CB    1 
ATOM   7858  O  OG    . SER L  3 31  ? 96.164  45.042  123.734 1.00 17.54 ? 31   SER D OG    1 
ATOM   7859  N  N     . ASN L  3 32  ? 92.922  44.269  122.332 1.00 14.69 ? 32   ASN D N     1 
ATOM   7860  C  CA    . ASN L  3 32  ? 91.528  44.699  122.435 1.00 13.62 ? 32   ASN D CA    1 
ATOM   7861  C  C     . ASN L  3 32  ? 90.634  43.759  121.611 1.00 13.39 ? 32   ASN D C     1 
ATOM   7862  O  O     . ASN L  3 32  ? 89.431  43.988  121.489 1.00 14.56 ? 32   ASN D O     1 
ATOM   7863  C  CB    . ASN L  3 32  ? 91.317  46.160  122.005 1.00 13.65 ? 32   ASN D CB    1 
ATOM   7864  C  CG    . ASN L  3 32  ? 91.686  46.414  120.563 1.00 17.33 ? 32   ASN D CG    1 
ATOM   7865  O  OD1   . ASN L  3 32  ? 92.563  45.747  120.004 1.00 17.04 ? 32   ASN D OD1   1 
ATOM   7866  N  ND2   . ASN L  3 32  ? 91.039  47.398  119.962 1.00 13.70 ? 32   ASN D ND2   1 
ATOM   7867  N  N     . ALA L  3 33  ? 91.223  42.680  121.074 1.00 14.54 ? 33   ALA D N     1 
ATOM   7868  C  CA    . ALA L  3 33  ? 90.463  41.703  120.297 1.00 13.70 ? 33   ALA D CA    1 
ATOM   7869  C  C     . ALA L  3 33  ? 89.959  40.548  121.148 1.00 16.26 ? 33   ALA D C     1 
ATOM   7870  O  O     . ALA L  3 33  ? 90.452  40.309  122.249 1.00 21.33 ? 33   ALA D O     1 
ATOM   7871  C  CB    . ALA L  3 33  ? 91.354  41.109  119.158 1.00 19.37 ? 33   ALA D CB    1 
ATOM   7872  N  N     . ASP L  3 34  ? 88.975  39.837  120.603 1.00 15.20 ? 34   ASP D N     1 
ATOM   7873  C  CA    . ASP L  3 34  ? 88.430  38.612  121.213 1.00 16.54 ? 34   ASP D CA    1 
ATOM   7874  C  C     . ASP L  3 34  ? 89.139  37.578  120.311 1.00 16.53 ? 34   ASP D C     1 
ATOM   7875  O  O     . ASP L  3 34  ? 88.768  37.422  119.158 1.00 18.37 ? 34   ASP D O     1 
ATOM   7876  C  CB    . ASP L  3 34  ? 86.918  38.560  121.003 1.00 15.94 ? 34   ASP D CB    1 
ATOM   7877  C  CG    . ASP L  3 34  ? 86.301  37.238  121.452 1.00 15.74 ? 34   ASP D CG    1 
ATOM   7878  O  OD1   . ASP L  3 34  ? 87.057  36.335  121.870 1.00 19.57 ? 34   ASP D OD1   1 
ATOM   7879  O  OD2   . ASP L  3 34  ? 85.066  37.126  121.352 1.00 17.99 ? 34   ASP D OD2   1 
ATOM   7880  N  N     . GLY L  3 35  ? 90.189  36.931  120.829 1.00 21.88 ? 35   GLY D N     1 
ATOM   7881  C  CA    . GLY L  3 35  ? 90.962  35.976  120.046 1.00 25.71 ? 35   GLY D CA    1 
ATOM   7882  C  C     . GLY L  3 35  ? 90.217  34.816  119.404 1.00 29.62 ? 35   GLY D C     1 
ATOM   7883  O  O     . GLY L  3 35  ? 90.670  34.265  118.388 1.00 31.24 ? 35   GLY D O     1 
ATOM   7884  N  N     . SER L  3 36  ? 89.078  34.442  119.984 1.00 25.32 ? 36   SER D N     1 
ATOM   7885  C  CA    . SER L  3 36  ? 88.259  33.344  119.449 1.00 29.69 ? 36   SER D CA    1 
ATOM   7886  C  C     . SER L  3 36  ? 87.425  33.822  118.269 1.00 27.44 ? 36   SER D C     1 
ATOM   7887  O  O     . SER L  3 36  ? 86.838  33.031  117.537 1.00 27.33 ? 36   SER D O     1 
ATOM   7888  C  CB    . SER L  3 36  ? 87.287  32.844  120.531 1.00 29.53 ? 36   SER D CB    1 
ATOM   7889  O  OG    . SER L  3 36  ? 87.962  32.650  121.762 1.00 39.23 ? 36   SER D OG    1 
ATOM   7890  N  N     . ASN L  3 37  ? 87.371  35.138  118.093 1.00 22.51 ? 37   ASN D N     1 
ATOM   7891  C  CA    . ASN L  3 37  ? 86.547  35.764  117.072 1.00 20.44 ? 37   ASN D CA    1 
ATOM   7892  C  C     . ASN L  3 37  ? 87.360  36.196  115.861 1.00 20.31 ? 37   ASN D C     1 
ATOM   7893  O  O     . ASN L  3 37  ? 88.130  37.157  115.937 1.00 20.83 ? 37   ASN D O     1 
ATOM   7894  C  CB    . ASN L  3 37  ? 85.879  36.986  117.709 1.00 19.77 ? 37   ASN D CB    1 
ATOM   7895  C  CG    . ASN L  3 37  ? 84.795  37.578  116.863 1.00 21.84 ? 37   ASN D CG    1 
ATOM   7896  O  OD1   . ASN L  3 37  ? 85.009  37.976  115.724 1.00 22.37 ? 37   ASN D OD1   1 
ATOM   7897  N  ND2   . ASN L  3 37  ? 83.598  37.650  117.426 1.00 33.59 ? 37   ASN D ND2   1 
ATOM   7898  N  N     . THR L  3 38  ? 87.178  35.508  114.737 1.00 17.96 ? 38   THR D N     1 
ATOM   7899  C  CA    . THR L  3 38  ? 87.946  35.842  113.535 1.00 18.29 ? 38   THR D CA    1 
ATOM   7900  C  C     . THR L  3 38  ? 87.907  37.317  113.130 1.00 17.50 ? 38   THR D C     1 
ATOM   7901  O  O     . THR L  3 38  ? 88.956  37.932  112.898 1.00 18.46 ? 38   THR D O     1 
ATOM   7902  C  CB    . THR L  3 38  ? 87.457  34.990  112.335 1.00 20.95 ? 38   THR D CB    1 
ATOM   7903  O  OG1   . THR L  3 38  ? 87.629  33.614  112.675 1.00 22.52 ? 38   THR D OG1   1 
ATOM   7904  C  CG2   . THR L  3 38  ? 88.219  35.335  111.048 1.00 22.59 ? 38   THR D CG2   1 
ATOM   7905  N  N     . ARG L  3 39  ? 86.712  37.893  113.030 1.00 16.57 ? 39   ARG D N     1 
ATOM   7906  C  CA    . ARG L  3 39  ? 86.629  39.292  112.601 1.00 15.63 ? 39   ARG D CA    1 
ATOM   7907  C  C     . ARG L  3 39  ? 87.213  40.256  113.613 1.00 16.65 ? 39   ARG D C     1 
ATOM   7908  O  O     . ARG L  3 39  ? 87.830  41.242  113.228 1.00 16.52 ? 39   ARG D O     1 
ATOM   7909  C  CB    . ARG L  3 39  ? 85.187  39.651  112.236 1.00 20.18 ? 39   ARG D CB    1 
ATOM   7910  C  CG    . ARG L  3 39  ? 84.755  38.849  110.984 1.00 30.85 ? 39   ARG D CG    1 
ATOM   7911  C  CD    . ARG L  3 39  ? 83.444  39.289  110.338 1.00 35.38 ? 39   ARG D CD    1 
ATOM   7912  N  NE    . ARG L  3 39  ? 83.468  38.914  108.919 1.00 44.63 ? 39   ARG D NE    1 
ATOM   7913  C  CZ    . ARG L  3 39  ? 83.469  37.659  108.462 1.00 47.83 ? 39   ARG D CZ    1 
ATOM   7914  N  NH1   . ARG L  3 39  ? 83.426  36.630  109.303 1.00 45.62 ? 39   ARG D NH1   1 
ATOM   7915  N  NH2   . ARG L  3 39  ? 83.572  37.427  107.157 1.00 49.78 ? 39   ARG D NH2   1 
ATOM   7916  N  N     . SER L  3 40  ? 87.044  39.958  114.904 1.00 14.99 ? 40   SER D N     1 
ATOM   7917  C  CA    . SER L  3 40  ? 87.611  40.793  115.951 1.00 16.32 ? 40   SER D CA    1 
ATOM   7918  C  C     . SER L  3 40  ? 89.139  40.795  115.813 1.00 15.02 ? 40   SER D C     1 
ATOM   7919  O  O     . SER L  3 40  ? 89.794  41.827  115.839 1.00 13.54 ? 40   SER D O     1 
ATOM   7920  C  CB    . SER L  3 40  ? 87.215  40.229  117.327 1.00 14.11 ? 40   SER D CB    1 
ATOM   7921  O  OG    . SER L  3 40  ? 87.696  41.075  118.367 1.00 15.34 ? 40   SER D OG    1 
ATOM   7922  N  N     . PHE L  3 41  ? 89.699  39.595  115.634 1.00 15.08 ? 41   PHE D N     1 
ATOM   7923  C  CA    . PHE L  3 41  ? 91.138  39.433  115.499 1.00 13.36 ? 41   PHE D CA    1 
ATOM   7924  C  C     . PHE L  3 41  ? 91.659  40.253  114.315 1.00 15.92 ? 41   PHE D C     1 
ATOM   7925  O  O     . PHE L  3 41  ? 92.606  41.038  114.450 1.00 15.35 ? 41   PHE D O     1 
ATOM   7926  C  CB    . PHE L  3 41  ? 91.433  37.922  115.309 1.00 14.84 ? 41   PHE D CB    1 
ATOM   7927  C  CG    . PHE L  3 41  ? 92.904  37.583  115.133 1.00 15.72 ? 41   PHE D CG    1 
ATOM   7928  C  CD1   . PHE L  3 41  ? 93.590  36.832  116.094 1.00 15.59 ? 41   PHE D CD1   1 
ATOM   7929  C  CD2   . PHE L  3 41  ? 93.582  37.961  113.973 1.00 18.05 ? 41   PHE D CD2   1 
ATOM   7930  C  CE1   . PHE L  3 41  ? 94.940  36.472  115.899 1.00 14.49 ? 41   PHE D CE1   1 
ATOM   7931  C  CE2   . PHE L  3 41  ? 94.919  37.596  113.773 1.00 17.02 ? 41   PHE D CE2   1 
ATOM   7932  C  CZ    . PHE L  3 41  ? 95.589  36.860  114.733 1.00 16.35 ? 41   PHE D CZ    1 
ATOM   7933  N  N     . ASN L  3 42  ? 91.026  40.085  113.155 1.00 16.28 ? 42   ASN D N     1 
ATOM   7934  C  CA    . ASN L  3 42  ? 91.493  40.787  111.971 1.00 17.30 ? 42   ASN D CA    1 
ATOM   7935  C  C     . ASN L  3 42  ? 91.297  42.291  111.986 1.00 17.62 ? 42   ASN D C     1 
ATOM   7936  O  O     . ASN L  3 42  ? 92.156  43.030  111.511 1.00 16.96 ? 42   ASN D O     1 
ATOM   7937  C  CB    . ASN L  3 42  ? 90.890  40.161  110.707 1.00 15.26 ? 42   ASN D CB    1 
ATOM   7938  C  CG    . ASN L  3 42  ? 91.469  38.778  110.449 1.00 18.13 ? 42   ASN D CG    1 
ATOM   7939  O  OD1   . ASN L  3 42  ? 92.674  38.591  110.542 1.00 24.51 ? 42   ASN D OD1   1 
ATOM   7940  N  ND2   . ASN L  3 42  ? 90.625  37.815  110.139 1.00 20.15 ? 42   ASN D ND2   1 
ATOM   7941  N  N     . ILE L  3 43  ? 90.171  42.747  112.514 1.00 16.22 ? 43   ILE D N     1 
ATOM   7942  C  CA    . ILE L  3 43  ? 89.930  44.188  112.593 1.00 14.95 ? 43   ILE D CA    1 
ATOM   7943  C  C     . ILE L  3 43  ? 90.931  44.813  113.573 1.00 15.00 ? 43   ILE D C     1 
ATOM   7944  O  O     . ILE L  3 43  ? 91.524  45.843  113.275 1.00 15.15 ? 43   ILE D O     1 
ATOM   7945  C  CB    . ILE L  3 43  ? 88.494  44.497  113.081 1.00 14.25 ? 43   ILE D CB    1 
ATOM   7946  C  CG1   . ILE L  3 43  ? 87.475  44.090  112.004 1.00 15.82 ? 43   ILE D CG1   1 
ATOM   7947  C  CG2   . ILE L  3 43  ? 88.342  45.989  113.385 1.00 13.18 ? 43   ILE D CG2   1 
ATOM   7948  C  CD1   . ILE L  3 43  ? 86.022  44.038  112.537 1.00 15.61 ? 43   ILE D CD1   1 
ATOM   7949  N  N     . ALA L  3 44  ? 91.122  44.175  114.733 1.00 14.59 ? 44   ALA D N     1 
ATOM   7950  C  CA    . ALA L  3 44  ? 92.031  44.697  115.738 1.00 14.23 ? 44   ALA D CA    1 
ATOM   7951  C  C     . ALA L  3 44  ? 93.471  44.746  115.234 1.00 14.85 ? 44   ALA D C     1 
ATOM   7952  O  O     . ALA L  3 44  ? 94.214  45.674  115.552 1.00 17.08 ? 44   ALA D O     1 
ATOM   7953  C  CB    . ALA L  3 44  ? 91.941  43.859  117.027 1.00 15.57 ? 44   ALA D CB    1 
ATOM   7954  N  N     . LYS L  3 45  ? 93.861  43.721  114.465 1.00 14.28 ? 45   LYS D N     1 
ATOM   7955  C  CA    . LYS L  3 45  ? 95.212  43.668  113.908 1.00 13.69 ? 45   LYS D CA    1 
ATOM   7956  C  C     . LYS L  3 45  ? 95.384  44.820  112.918 1.00 14.87 ? 45   LYS D C     1 
ATOM   7957  O  O     . LYS L  3 45  ? 96.415  45.478  112.926 1.00 17.28 ? 45   LYS D O     1 
ATOM   7958  C  CB    . LYS L  3 45  ? 95.433  42.328  113.192 1.00 18.75 ? 45   LYS D CB    1 
ATOM   7959  C  CG    . LYS L  3 45  ? 96.735  42.230  112.424 1.00 23.11 ? 45   LYS D CG    1 
ATOM   7960  C  CD    . LYS L  3 45  ? 96.682  41.034  111.483 1.00 33.78 ? 45   LYS D CD    1 
ATOM   7961  C  CE    . LYS L  3 45  ? 97.953  40.920  110.659 1.00 40.13 ? 45   LYS D CE    1 
ATOM   7962  N  NZ    . LYS L  3 45  ? 99.118  40.680  111.549 1.00 45.06 ? 45   LYS D NZ    1 
ATOM   7963  N  N     . GLY L  3 46  ? 94.367  45.053  112.080 1.00 17.67 ? 46   GLY D N     1 
ATOM   7964  C  CA    . GLY L  3 46  ? 94.419  46.137  111.096 1.00 15.39 ? 46   GLY D CA    1 
ATOM   7965  C  C     . GLY L  3 46  ? 94.588  47.491  111.776 1.00 19.59 ? 46   GLY D C     1 
ATOM   7966  O  O     . GLY L  3 46  ? 95.388  48.338  111.361 1.00 17.68 ? 46   GLY D O     1 
ATOM   7967  N  N     . ILE L  3 47  ? 93.836  47.700  112.850 1.00 16.52 ? 47   ILE D N     1 
ATOM   7968  C  CA    . ILE L  3 47  ? 93.927  48.960  113.585 1.00 16.27 ? 47   ILE D CA    1 
ATOM   7969  C  C     . ILE L  3 47  ? 95.308  49.122  114.221 1.00 15.78 ? 47   ILE D C     1 
ATOM   7970  O  O     . ILE L  3 47  ? 95.902  50.193  114.146 1.00 17.22 ? 47   ILE D O     1 
ATOM   7971  C  CB    . ILE L  3 47  ? 92.819  49.050  114.674 1.00 13.38 ? 47   ILE D CB    1 
ATOM   7972  C  CG1   . ILE L  3 47  ? 91.450  49.124  114.014 1.00 16.83 ? 47   ILE D CG1   1 
ATOM   7973  C  CG2   . ILE L  3 47  ? 93.064  50.265  115.569 1.00 15.89 ? 47   ILE D CG2   1 
ATOM   7974  C  CD1   . ILE L  3 47  ? 90.285  49.125  115.016 1.00 15.48 ? 47   ILE D CD1   1 
ATOM   7975  N  N     . ALA L  3 48  ? 95.830  48.054  114.834 1.00 15.44 ? 48   ALA D N     1 
ATOM   7976  C  CA    . ALA L  3 48  ? 97.139  48.091  115.460 1.00 16.93 ? 48   ALA D CA    1 
ATOM   7977  C  C     . ALA L  3 48  ? 98.211  48.431  114.400 1.00 17.91 ? 48   ALA D C     1 
ATOM   7978  O  O     . ALA L  3 48  ? 99.109  49.220  114.651 1.00 19.44 ? 48   ALA D O     1 
ATOM   7979  C  CB    . ALA L  3 48  ? 97.425  46.751  116.127 1.00 20.46 ? 48   ALA D CB    1 
ATOM   7980  N  N     . ASP L  3 49  ? 98.095  47.836  113.221 1.00 18.26 ? 49   ASP D N     1 
ATOM   7981  C  CA    . ASP L  3 49  ? 99.028  48.140  112.143 1.00 19.76 ? 49   ASP D CA    1 
ATOM   7982  C  C     . ASP L  3 49  ? 98.961  49.628  111.761 1.00 19.60 ? 49   ASP D C     1 
ATOM   7983  O  O     . ASP L  3 49  ? 100.014 50.279  111.584 1.00 20.21 ? 49   ASP D O     1 
ATOM   7984  C  CB    . ASP L  3 49  ? 98.719  47.289  110.909 1.00 21.05 ? 49   ASP D CB    1 
ATOM   7985  C  CG    . ASP L  3 49  ? 99.221  45.857  111.041 1.00 27.74 ? 49   ASP D CG    1 
ATOM   7986  O  OD1   . ASP L  3 49  ? 100.068 45.573  111.930 1.00 30.35 ? 49   ASP D OD1   1 
ATOM   7987  O  OD2   . ASP L  3 49  ? 98.776  45.017  110.230 1.00 32.74 ? 49   ASP D OD2   1 
ATOM   7988  N  N     . LEU L  3 50  ? 97.747  50.173  111.632 1.00 16.03 ? 50   LEU D N     1 
ATOM   7989  C  CA    . LEU L  3 50  ? 97.600  51.593  111.262 1.00 19.43 ? 50   LEU D CA    1 
ATOM   7990  C  C     . LEU L  3 50  ? 98.048  52.538  112.389 1.00 22.22 ? 50   LEU D C     1 
ATOM   7991  O  O     . LEU L  3 50  ? 98.295  53.735  112.162 1.00 19.65 ? 50   LEU D O     1 
ATOM   7992  C  CB    . LEU L  3 50  ? 96.162  51.894  110.851 1.00 18.07 ? 50   LEU D CB    1 
ATOM   7993  C  CG    . LEU L  3 50  ? 95.759  51.241  109.518 1.00 18.68 ? 50   LEU D CG    1 
ATOM   7994  C  CD1   . LEU L  3 50  ? 94.267  51.357  109.283 1.00 20.07 ? 50   LEU D CD1   1 
ATOM   7995  C  CD2   . LEU L  3 50  ? 96.550  51.912  108.402 1.00 23.80 ? 50   LEU D CD2   1 
ATOM   7996  N  N     . LEU L  3 51  ? 98.128  52.010  113.608 1.00 18.85 ? 51   LEU D N     1 
ATOM   7997  C  CA    . LEU L  3 51  ? 98.631  52.795  114.743 1.00 18.96 ? 51   LEU D CA    1 
ATOM   7998  C  C     . LEU L  3 51  ? 100.150 52.583  114.863 1.00 21.49 ? 51   LEU D C     1 
ATOM   7999  O  O     . LEU L  3 51  ? 100.792 53.128  115.755 1.00 19.95 ? 51   LEU D O     1 
ATOM   8000  C  CB    . LEU L  3 51  ? 97.962  52.358  116.052 1.00 17.62 ? 51   LEU D CB    1 
ATOM   8001  C  CG    . LEU L  3 51  ? 96.812  53.255  116.510 1.00 20.15 ? 51   LEU D CG    1 
ATOM   8002  C  CD1   . LEU L  3 51  ? 95.779  53.366  115.435 1.00 19.75 ? 51   LEU D CD1   1 
ATOM   8003  C  CD2   . LEU L  3 51  ? 96.190  52.656  117.774 1.00 18.81 ? 51   LEU D CD2   1 
ATOM   8004  N  N     . HIS L  3 52  ? 100.703 51.776  113.963 1.00 21.11 ? 52   HIS D N     1 
ATOM   8005  C  CA    . HIS L  3 52  ? 102.137 51.456  113.949 1.00 23.15 ? 52   HIS D CA    1 
ATOM   8006  C  C     . HIS L  3 52  ? 102.574 50.742  115.222 1.00 22.97 ? 52   HIS D C     1 
ATOM   8007  O  O     . HIS L  3 52  ? 103.653 50.999  115.780 1.00 24.60 ? 52   HIS D O     1 
ATOM   8008  C  CB    . HIS L  3 52  ? 102.989 52.717  113.739 1.00 25.40 ? 52   HIS D CB    1 
ATOM   8009  C  CG    . HIS L  3 52  ? 103.017 53.184  112.320 1.00 31.81 ? 52   HIS D CG    1 
ATOM   8010  N  ND1   . HIS L  3 52  ? 101.878 53.543  111.635 1.00 37.69 ? 52   HIS D ND1   1 
ATOM   8011  C  CD2   . HIS L  3 52  ? 104.039 53.316  111.444 1.00 37.90 ? 52   HIS D CD2   1 
ATOM   8012  C  CE1   . HIS L  3 52  ? 102.195 53.877  110.397 1.00 39.14 ? 52   HIS D CE1   1 
ATOM   8013  N  NE2   . HIS L  3 52  ? 103.501 53.747  110.253 1.00 39.66 ? 52   HIS D NE2   1 
ATOM   8014  N  N     . SER L  3 53  ? 101.735 49.819  115.676 1.00 22.54 ? 53   SER D N     1 
ATOM   8015  C  CA    . SER L  3 53  ? 102.039 49.065  116.887 1.00 22.89 ? 53   SER D CA    1 
ATOM   8016  C  C     . SER L  3 53  ? 103.017 47.917  116.575 1.00 26.20 ? 53   SER D C     1 
ATOM   8017  O  O     . SER L  3 53  ? 102.781 47.148  115.639 1.00 26.11 ? 53   SER D O     1 
ATOM   8018  C  CB    . SER L  3 53  ? 100.747 48.492  117.474 1.00 23.12 ? 53   SER D CB    1 
ATOM   8019  O  OG    . SER L  3 53  ? 101.021 47.685  118.613 1.00 23.58 ? 53   SER D OG    1 
ATOM   8020  N  N     . GLU L  3 54  ? 104.094 47.798  117.346 1.00 26.76 ? 54   GLU D N     1 
ATOM   8021  C  CA    . GLU L  3 54  ? 105.045 46.712  117.103 1.00 31.25 ? 54   GLU D CA    1 
ATOM   8022  C  C     . GLU L  3 54  ? 105.357 45.843  118.320 1.00 28.96 ? 54   GLU D C     1 
ATOM   8023  O  O     . GLU L  3 54  ? 105.850 44.727  118.168 1.00 31.34 ? 54   GLU D O     1 
ATOM   8024  C  CB    . GLU L  3 54  ? 106.360 47.261  116.511 1.00 38.20 ? 54   GLU D CB    1 
ATOM   8025  C  CG    . GLU L  3 54  ? 106.289 47.631  115.015 1.00 44.18 ? 54   GLU D CG    1 
ATOM   8026  C  CD    . GLU L  3 54  ? 107.627 48.148  114.455 1.00 49.59 ? 54   GLU D CD    1 
ATOM   8027  O  OE1   . GLU L  3 54  ? 108.642 47.419  114.531 1.00 53.82 ? 54   GLU D OE1   1 
ATOM   8028  O  OE2   . GLU L  3 54  ? 107.663 49.283  113.933 1.00 50.10 ? 54   GLU D OE2   1 
ATOM   8029  N  N     . THR L  3 55  ? 105.056 46.318  119.521 1.00 25.58 ? 55   THR D N     1 
ATOM   8030  C  CA    . THR L  3 55  ? 105.345 45.546  120.728 1.00 24.83 ? 55   THR D CA    1 
ATOM   8031  C  C     . THR L  3 55  ? 104.594 44.216  120.836 1.00 28.77 ? 55   THR D C     1 
ATOM   8032  O  O     . THR L  3 55  ? 103.394 44.138  120.551 1.00 23.36 ? 55   THR D O     1 
ATOM   8033  C  CB    . THR L  3 55  ? 105.022 46.332  121.999 1.00 25.31 ? 55   THR D CB    1 
ATOM   8034  O  OG1   . THR L  3 55  ? 105.755 47.561  122.003 1.00 30.53 ? 55   THR D OG1   1 
ATOM   8035  C  CG2   . THR L  3 55  ? 105.389 45.507  123.253 1.00 23.67 ? 55   THR D CG2   1 
ATOM   8036  N  N     . VAL L  3 56  ? 105.321 43.172  121.234 1.00 24.90 ? 56   VAL D N     1 
ATOM   8037  C  CA    . VAL L  3 56  ? 104.740 41.848  121.450 1.00 25.89 ? 56   VAL D CA    1 
ATOM   8038  C  C     . VAL L  3 56  ? 104.812 41.628  122.955 1.00 27.76 ? 56   VAL D C     1 
ATOM   8039  O  O     . VAL L  3 56  ? 105.882 41.742  123.561 1.00 29.80 ? 56   VAL D O     1 
ATOM   8040  C  CB    . VAL L  3 56  ? 105.536 40.734  120.725 1.00 24.60 ? 56   VAL D CB    1 
ATOM   8041  C  CG1   . VAL L  3 56  ? 104.923 39.342  121.036 1.00 25.59 ? 56   VAL D CG1   1 
ATOM   8042  C  CG2   . VAL L  3 56  ? 105.501 40.974  119.242 1.00 24.15 ? 56   VAL D CG2   1 
ATOM   8043  N  N     . SER L  3 57  ? 103.666 41.349  123.566 1.00 23.39 ? 57   SER D N     1 
ATOM   8044  C  CA    . SER L  3 57  ? 103.586 41.116  124.994 1.00 24.61 ? 57   SER D CA    1 
ATOM   8045  C  C     . SER L  3 57  ? 102.261 40.432  125.288 1.00 24.76 ? 57   SER D C     1 
ATOM   8046  O  O     . SER L  3 57  ? 101.328 40.502  124.482 1.00 20.81 ? 57   SER D O     1 
ATOM   8047  C  CB    . SER L  3 57  ? 103.665 42.435  125.765 1.00 27.59 ? 57   SER D CB    1 
ATOM   8048  O  OG    . SER L  3 57  ? 102.509 43.220  125.553 1.00 34.78 ? 57   SER D OG    1 
ATOM   8049  N  N     . GLU L  3 58  ? 102.188 39.750  126.428 1.00 23.59 ? 58   GLU D N     1 
ATOM   8050  C  CA    . GLU L  3 58  ? 100.964 39.072  126.803 1.00 25.12 ? 58   GLU D CA    1 
ATOM   8051  C  C     . GLU L  3 58  ? 99.920  40.116  127.135 1.00 20.63 ? 58   GLU D C     1 
ATOM   8052  O  O     . GLU L  3 58  ? 100.234 41.218  127.566 1.00 20.40 ? 58   GLU D O     1 
ATOM   8053  C  CB    . GLU L  3 58  ? 101.203 38.173  128.021 1.00 26.90 ? 58   GLU D CB    1 
ATOM   8054  C  CG    . GLU L  3 58  ? 101.840 36.833  127.673 1.00 35.65 ? 58   GLU D CG    1 
ATOM   8055  C  CD    . GLU L  3 58  ? 100.926 35.949  126.823 1.00 38.41 ? 58   GLU D CD    1 
ATOM   8056  O  OE1   . GLU L  3 58  ? 99.854  35.539  127.309 1.00 43.63 ? 58   GLU D OE1   1 
ATOM   8057  O  OE2   . GLU L  3 58  ? 101.276 35.665  125.665 1.00 39.74 ? 58   GLU D OE2   1 
ATOM   8058  N  N     . ARG L  3 59  ? 98.671  39.754  126.905 1.00 20.03 ? 59   ARG D N     1 
ATOM   8059  C  CA    . ARG L  3 59  ? 97.548  40.624  127.194 1.00 18.32 ? 59   ARG D CA    1 
ATOM   8060  C  C     . ARG L  3 59  ? 97.580  40.989  128.679 1.00 17.11 ? 59   ARG D C     1 
ATOM   8061  O  O     . ARG L  3 59  ? 97.857  40.136  129.527 1.00 18.93 ? 59   ARG D O     1 
ATOM   8062  C  CB    . ARG L  3 59  ? 96.281  39.853  126.888 1.00 19.27 ? 59   ARG D CB    1 
ATOM   8063  C  CG    . ARG L  3 59  ? 95.022  40.656  126.875 1.00 20.52 ? 59   ARG D CG    1 
ATOM   8064  C  CD    . ARG L  3 59  ? 93.893  39.667  126.602 1.00 23.84 ? 59   ARG D CD    1 
ATOM   8065  N  NE    . ARG L  3 59  ? 92.737  40.349  126.096 1.00 31.31 ? 59   ARG D NE    1 
ATOM   8066  C  CZ    . ARG L  3 59  ? 92.304  40.281  124.845 1.00 22.37 ? 59   ARG D CZ    1 
ATOM   8067  N  NH1   . ARG L  3 59  ? 92.922  39.541  123.917 1.00 22.42 ? 59   ARG D NH1   1 
ATOM   8068  N  NH2   . ARG L  3 59  ? 91.249  40.972  124.530 1.00 24.03 ? 59   ARG D NH2   1 
ATOM   8069  N  N     . LEU L  3 60  ? 97.285  42.237  129.000 1.00 18.20 ? 60   LEU D N     1 
ATOM   8070  C  CA    . LEU L  3 60  ? 97.274  42.620  130.407 1.00 18.77 ? 60   LEU D CA    1 
ATOM   8071  C  C     . LEU L  3 60  ? 95.966  42.159  131.045 1.00 18.01 ? 60   LEU D C     1 
ATOM   8072  O  O     . LEU L  3 60  ? 94.966  41.933  130.338 1.00 17.01 ? 60   LEU D O     1 
ATOM   8073  C  CB    . LEU L  3 60  ? 97.358  44.142  130.554 1.00 21.77 ? 60   LEU D CB    1 
ATOM   8074  C  CG    . LEU L  3 60  ? 98.566  44.855  129.942 1.00 21.14 ? 60   LEU D CG    1 
ATOM   8075  C  CD1   . LEU L  3 60  ? 98.503  46.336  130.318 1.00 21.22 ? 60   LEU D CD1   1 
ATOM   8076  C  CD2   . LEU L  3 60  ? 99.857  44.229  130.432 1.00 22.52 ? 60   LEU D CD2   1 
ATOM   8077  N  N     . PRO L  3 61  ? 95.961  41.975  132.384 1.00 18.32 ? 61   PRO D N     1 
ATOM   8078  C  CA    . PRO L  3 61  ? 94.735  41.566  133.069 1.00 18.13 ? 61   PRO D CA    1 
ATOM   8079  C  C     . PRO L  3 61  ? 93.644  42.608  132.717 1.00 14.07 ? 61   PRO D C     1 
ATOM   8080  O  O     . PRO L  3 61  ? 93.933  43.811  132.556 1.00 15.14 ? 61   PRO D O     1 
ATOM   8081  C  CB    . PRO L  3 61  ? 95.118  41.651  134.550 1.00 17.06 ? 61   PRO D CB    1 
ATOM   8082  C  CG    . PRO L  3 61  ? 96.593  41.307  134.558 1.00 14.85 ? 61   PRO D CG    1 
ATOM   8083  C  CD    . PRO L  3 61  ? 97.100  42.072  133.321 1.00 17.71 ? 61   PRO D CD    1 
ATOM   8084  N  N     . GLY L  3 62  ? 92.397  42.148  132.635 1.00 13.67 ? 62   GLY D N     1 
ATOM   8085  C  CA    . GLY L  3 62  ? 91.291  43.038  132.312 1.00 14.78 ? 62   GLY D CA    1 
ATOM   8086  C  C     . GLY L  3 62  ? 91.136  44.183  133.298 1.00 16.92 ? 62   GLY D C     1 
ATOM   8087  O  O     . GLY L  3 62  ? 90.748  45.279  132.913 1.00 15.07 ? 62   GLY D O     1 
ATOM   8088  N  N     . GLN L  3 63  ? 91.441  43.960  134.570 1.00 14.64 ? 63   GLN D N     1 
ATOM   8089  C  CA    . GLN L  3 63  ? 91.304  45.043  135.534 1.00 15.68 ? 63   GLN D CA    1 
ATOM   8090  C  C     . GLN L  3 63  ? 92.331  46.157  135.245 1.00 16.09 ? 63   GLN D C     1 
ATOM   8091  O  O     . GLN L  3 63  ? 92.065  47.327  135.478 1.00 16.17 ? 63   GLN D O     1 
ATOM   8092  C  CB    . GLN L  3 63  ? 91.518  44.507  136.965 1.00 18.14 ? 63   GLN D CB    1 
ATOM   8093  C  CG    . GLN L  3 63  ? 90.626  43.308  137.318 1.00 15.76 ? 63   GLN D CG    1 
ATOM   8094  C  CD    . GLN L  3 63  ? 91.208  41.932  136.972 1.00 15.79 ? 63   GLN D CD    1 
ATOM   8095  O  OE1   . GLN L  3 63  ? 92.075  41.777  136.111 1.00 15.98 ? 63   GLN D OE1   1 
ATOM   8096  N  NE2   . GLN L  3 63  ? 90.699  40.909  137.653 1.00 15.77 ? 63   GLN D NE2   1 
ATOM   8097  N  N     . THR L  3 64  ? 93.505  45.766  134.764 1.00 16.18 ? 64   THR D N     1 
ATOM   8098  C  CA    . THR L  3 64  ? 94.587  46.700  134.451 1.00 14.91 ? 64   THR D CA    1 
ATOM   8099  C  C     . THR L  3 64  ? 94.223  47.523  133.226 1.00 16.61 ? 64   THR D C     1 
ATOM   8100  O  O     . THR L  3 64  ? 94.298  48.750  133.257 1.00 15.95 ? 64   THR D O     1 
ATOM   8101  C  CB    . THR L  3 64  ? 95.877  45.940  134.156 1.00 16.49 ? 64   THR D CB    1 
ATOM   8102  O  OG1   . THR L  3 64  ? 96.177  45.085  135.270 1.00 16.70 ? 64   THR D OG1   1 
ATOM   8103  C  CG2   . THR L  3 64  ? 97.034  46.911  133.929 1.00 14.60 ? 64   THR D CG2   1 
ATOM   8104  N  N     . SER L  3 65  ? 93.817  46.850  132.148 1.00 15.32 ? 65   SER D N     1 
ATOM   8105  C  CA    . SER L  3 65  ? 93.440  47.583  130.929 1.00 15.81 ? 65   SER D CA    1 
ATOM   8106  C  C     . SER L  3 65  ? 92.200  48.475  131.123 1.00 16.17 ? 65   SER D C     1 
ATOM   8107  O  O     . SER L  3 65  ? 92.155  49.595  130.593 1.00 15.19 ? 65   SER D O     1 
ATOM   8108  C  CB    . SER L  3 65  ? 93.216  46.595  129.758 1.00 15.76 ? 65   SER D CB    1 
ATOM   8109  O  OG    . SER L  3 65  ? 92.212  45.640  130.064 1.00 15.58 ? 65   SER D OG    1 
ATOM   8110  N  N     . GLY L  3 66  ? 91.217  48.000  131.898 1.00 13.82 ? 66   GLY D N     1 
ATOM   8111  C  CA    . GLY L  3 66  ? 90.021  48.798  132.159 1.00 13.73 ? 66   GLY D CA    1 
ATOM   8112  C  C     . GLY L  3 66  ? 90.386  50.101  132.881 1.00 15.51 ? 66   GLY D C     1 
ATOM   8113  O  O     . GLY L  3 66  ? 89.957  51.196  132.510 1.00 15.19 ? 66   GLY D O     1 
ATOM   8114  N  N     . ASN L  3 67  ? 91.195  49.992  133.930 1.00 14.23 ? 67   ASN D N     1 
ATOM   8115  C  CA    . ASN L  3 67  ? 91.609  51.182  134.672 1.00 14.79 ? 67   ASN D CA    1 
ATOM   8116  C  C     . ASN L  3 67  ? 92.506  52.091  133.833 1.00 14.41 ? 67   ASN D C     1 
ATOM   8117  O  O     . ASN L  3 67  ? 92.314  53.314  133.827 1.00 14.20 ? 67   ASN D O     1 
ATOM   8118  C  CB    . ASN L  3 67  ? 92.358  50.787  135.951 1.00 15.63 ? 67   ASN D CB    1 
ATOM   8119  C  CG    . ASN L  3 67  ? 92.802  52.012  136.754 1.00 19.63 ? 67   ASN D CG    1 
ATOM   8120  O  OD1   . ASN L  3 67  ? 91.974  52.728  137.303 1.00 18.44 ? 67   ASN D OD1   1 
ATOM   8121  N  ND2   . ASN L  3 67  ? 94.109  52.267  136.787 1.00 21.13 ? 67   ASN D ND2   1 
ATOM   8122  N  N     . ALA L  3 68  ? 93.470  51.513  133.117 1.00 14.35 ? 68   ALA D N     1 
ATOM   8123  C  CA    . ALA L  3 68  ? 94.384  52.331  132.305 1.00 15.92 ? 68   ALA D CA    1 
ATOM   8124  C  C     . ALA L  3 68  ? 93.616  53.054  131.210 1.00 17.18 ? 68   ALA D C     1 
ATOM   8125  O  O     . ALA L  3 68  ? 93.890  54.218  130.933 1.00 16.02 ? 68   ALA D O     1 
ATOM   8126  C  CB    . ALA L  3 68  ? 95.494  51.473  131.671 1.00 16.80 ? 68   ALA D CB    1 
ATOM   8127  N  N     . PHE L  3 69  ? 92.649  52.371  130.586 1.00 14.73 ? 69   PHE D N     1 
ATOM   8128  C  CA    . PHE L  3 69  ? 91.893  53.012  129.510 1.00 14.16 ? 69   PHE D CA    1 
ATOM   8129  C  C     . PHE L  3 69  ? 91.115  54.221  130.049 1.00 14.68 ? 69   PHE D C     1 
ATOM   8130  O  O     . PHE L  3 69  ? 91.073  55.300  129.414 1.00 13.86 ? 69   PHE D O     1 
ATOM   8131  C  CB    . PHE L  3 69  ? 90.967  51.978  128.819 1.00 12.63 ? 69   PHE D CB    1 
ATOM   8132  C  CG    . PHE L  3 69  ? 90.240  52.535  127.617 1.00 13.82 ? 69   PHE D CG    1 
ATOM   8133  C  CD1   . PHE L  3 69  ? 90.952  53.038  126.538 1.00 13.90 ? 69   PHE D CD1   1 
ATOM   8134  C  CD2   . PHE L  3 69  ? 88.848  52.489  127.545 1.00 14.34 ? 69   PHE D CD2   1 
ATOM   8135  C  CE1   . PHE L  3 69  ? 90.286  53.487  125.386 1.00 13.45 ? 69   PHE D CE1   1 
ATOM   8136  C  CE2   . PHE L  3 69  ? 88.174  52.932  126.411 1.00 13.40 ? 69   PHE D CE2   1 
ATOM   8137  C  CZ    . PHE L  3 69  ? 88.914  53.437  125.313 1.00 12.56 ? 69   PHE D CZ    1 
ATOM   8138  N  N     . GLU L  3 70  ? 90.523  54.077  131.238 1.00 15.36 ? 70   GLU D N     1 
ATOM   8139  C  CA    . GLU L  3 70  ? 89.815  55.197  131.862 1.00 13.74 ? 70   GLU D CA    1 
ATOM   8140  C  C     . GLU L  3 70  ? 90.787  56.363  132.103 1.00 15.20 ? 70   GLU D C     1 
ATOM   8141  O  O     . GLU L  3 70  ? 90.485  57.524  131.810 1.00 14.20 ? 70   GLU D O     1 
ATOM   8142  C  CB    . GLU L  3 70  ? 89.254  54.805  133.229 1.00 15.68 ? 70   GLU D CB    1 
ATOM   8143  C  CG    . GLU L  3 70  ? 88.005  53.970  133.200 1.00 15.95 ? 70   GLU D CG    1 
ATOM   8144  C  CD    . GLU L  3 70  ? 87.591  53.475  134.592 1.00 23.31 ? 70   GLU D CD    1 
ATOM   8145  O  OE1   . GLU L  3 70  ? 88.109  53.991  135.605 1.00 18.88 ? 70   GLU D OE1   1 
ATOM   8146  O  OE2   . GLU L  3 70  ? 86.737  52.575  134.666 1.00 19.75 ? 70   GLU D OE2   1 
ATOM   8147  N  N     . ALA L  3 71  ? 91.944  56.047  132.676 1.00 14.94 ? 71   ALA D N     1 
ATOM   8148  C  CA    . ALA L  3 71  ? 92.926  57.088  132.964 1.00 14.61 ? 71   ALA D CA    1 
ATOM   8149  C  C     . ALA L  3 71  ? 93.395  57.822  131.719 1.00 14.20 ? 71   ALA D C     1 
ATOM   8150  O  O     . ALA L  3 71  ? 93.456  59.047  131.710 1.00 15.22 ? 71   ALA D O     1 
ATOM   8151  C  CB    . ALA L  3 71  ? 94.145  56.476  133.714 1.00 14.74 ? 71   ALA D CB    1 
ATOM   8152  N  N     . ILE L  3 72  ? 93.724  57.076  130.667 1.00 14.05 ? 72   ILE D N     1 
ATOM   8153  C  CA    . ILE L  3 72  ? 94.211  57.688  129.434 1.00 15.09 ? 72   ILE D CA    1 
ATOM   8154  C  C     . ILE L  3 72  ? 93.122  58.506  128.733 1.00 15.09 ? 72   ILE D C     1 
ATOM   8155  O  O     . ILE L  3 72  ? 93.397  59.596  128.204 1.00 14.87 ? 72   ILE D O     1 
ATOM   8156  C  CB    . ILE L  3 72  ? 94.829  56.575  128.545 1.00 13.48 ? 72   ILE D CB    1 
ATOM   8157  C  CG1   . ILE L  3 72  ? 96.072  56.021  129.283 1.00 17.43 ? 72   ILE D CG1   1 
ATOM   8158  C  CG2   . ILE L  3 72  ? 95.161  57.100  127.132 1.00 18.21 ? 72   ILE D CG2   1 
ATOM   8159  C  CD1   . ILE L  3 72  ? 96.637  54.722  128.733 1.00 18.09 ? 72   ILE D CD1   1 
ATOM   8160  N  N     . CYS L  3 73  ? 91.885  58.002  128.733 1.00 14.93 ? 73   CYS D N     1 
ATOM   8161  C  CA    . CYS L  3 73  ? 90.772  58.771  128.157 1.00 12.96 ? 73   CYS D CA    1 
ATOM   8162  C  C     . CYS L  3 73  ? 90.600  60.075  128.958 1.00 14.22 ? 73   CYS D C     1 
ATOM   8163  O  O     . CYS L  3 73  ? 90.381  61.130  128.390 1.00 15.38 ? 73   CYS D O     1 
ATOM   8164  C  CB    . CYS L  3 73  ? 89.466  57.985  128.255 1.00 13.93 ? 73   CYS D CB    1 
ATOM   8165  S  SG    . CYS L  3 73  ? 89.297  56.639  127.082 1.00 17.00 ? 73   CYS D SG    1 
ATOM   8166  N  N     . SER L  3 74  ? 90.711  59.982  130.283 1.00 13.21 ? 74   SER D N     1 
ATOM   8167  C  CA    . SER L  3 74  ? 90.547  61.166  131.138 1.00 13.54 ? 74   SER D CA    1 
ATOM   8168  C  C     . SER L  3 74  ? 91.592  62.235  130.772 1.00 16.64 ? 74   SER D C     1 
ATOM   8169  O  O     . SER L  3 74  ? 91.271  63.420  130.604 1.00 15.55 ? 74   SER D O     1 
ATOM   8170  C  CB    . SER L  3 74  ? 90.694  60.762  132.619 1.00 18.25 ? 74   SER D CB    1 
ATOM   8171  O  OG    . SER L  3 74  ? 90.411  61.859  133.471 1.00 26.40 ? 74   SER D OG    1 
ATOM   8172  N  N     . GLU L  3 75  ? 92.844  61.809  130.630 1.00 15.46 ? 75   GLU D N     1 
ATOM   8173  C  CA    . GLU L  3 75  ? 93.908  62.746  130.271 1.00 15.90 ? 75   GLU D CA    1 
ATOM   8174  C  C     . GLU L  3 75  ? 93.718  63.370  128.901 1.00 16.07 ? 75   GLU D C     1 
ATOM   8175  O  O     . GLU L  3 75  ? 94.012  64.545  128.714 1.00 15.93 ? 75   GLU D O     1 
ATOM   8176  C  CB    . GLU L  3 75  ? 95.264  62.041  130.350 1.00 17.21 ? 75   GLU D CB    1 
ATOM   8177  C  CG    . GLU L  3 75  ? 95.578  61.609  131.789 1.00 17.27 ? 75   GLU D CG    1 
ATOM   8178  C  CD    . GLU L  3 75  ? 96.800  60.719  131.908 1.00 28.74 ? 75   GLU D CD    1 
ATOM   8179  O  OE1   . GLU L  3 75  ? 97.391  60.351  130.874 1.00 26.13 ? 75   GLU D OE1   1 
ATOM   8180  O  OE2   . GLU L  3 75  ? 97.167  60.375  133.054 1.00 31.20 ? 75   GLU D OE2   1 
ATOM   8181  N  N     . PHE L  3 76  ? 93.237  62.594  127.933 1.00 14.86 ? 76   PHE D N     1 
ATOM   8182  C  CA    . PHE L  3 76  ? 92.993  63.143  126.607 1.00 15.30 ? 76   PHE D CA    1 
ATOM   8183  C  C     . PHE L  3 76  ? 91.889  64.200  126.686 1.00 16.24 ? 76   PHE D C     1 
ATOM   8184  O  O     . PHE L  3 76  ? 92.024  65.295  126.144 1.00 14.96 ? 76   PHE D O     1 
ATOM   8185  C  CB    . PHE L  3 76  ? 92.564  62.045  125.642 1.00 14.99 ? 76   PHE D CB    1 
ATOM   8186  C  CG    . PHE L  3 76  ? 91.995  62.575  124.360 1.00 15.93 ? 76   PHE D CG    1 
ATOM   8187  C  CD1   . PHE L  3 76  ? 92.833  63.054  123.358 1.00 16.27 ? 76   PHE D CD1   1 
ATOM   8188  C  CD2   . PHE L  3 76  ? 90.601  62.652  124.192 1.00 17.24 ? 76   PHE D CD2   1 
ATOM   8189  C  CE1   . PHE L  3 76  ? 92.288  63.614  122.193 1.00 17.02 ? 76   PHE D CE1   1 
ATOM   8190  C  CE2   . PHE L  3 76  ? 90.051  63.202  123.035 1.00 18.09 ? 76   PHE D CE2   1 
ATOM   8191  C  CZ    . PHE L  3 76  ? 90.892  63.684  122.034 1.00 18.42 ? 76   PHE D CZ    1 
ATOM   8192  N  N     . VAL L  3 77  ? 90.781  63.879  127.357 1.00 14.96 ? 77   VAL D N     1 
ATOM   8193  C  CA    . VAL L  3 77  ? 89.690  64.844  127.458 1.00 14.07 ? 77   VAL D CA    1 
ATOM   8194  C  C     . VAL L  3 77  ? 90.132  66.124  128.171 1.00 15.40 ? 77   VAL D C     1 
ATOM   8195  O  O     . VAL L  3 77  ? 89.822  67.224  127.734 1.00 15.98 ? 77   VAL D O     1 
ATOM   8196  C  CB    . VAL L  3 77  ? 88.462  64.212  128.191 1.00 13.33 ? 77   VAL D CB    1 
ATOM   8197  C  CG1   . VAL L  3 77  ? 87.415  65.269  128.509 1.00 14.33 ? 77   VAL D CG1   1 
ATOM   8198  C  CG2   . VAL L  3 77  ? 87.840  63.144  127.302 1.00 15.68 ? 77   VAL D CG2   1 
ATOM   8199  N  N     . GLN L  3 78  ? 90.866  65.971  129.264 1.00 14.40 ? 78   GLN D N     1 
ATOM   8200  C  CA    . GLN L  3 78  ? 91.341  67.126  130.011 1.00 16.53 ? 78   GLN D CA    1 
ATOM   8201  C  C     . GLN L  3 78  ? 92.220  68.014  129.127 1.00 16.19 ? 78   GLN D C     1 
ATOM   8202  O  O     . GLN L  3 78  ? 91.974  69.221  129.033 1.00 19.13 ? 78   GLN D O     1 
ATOM   8203  C  CB    . GLN L  3 78  ? 92.113  66.655  131.261 1.00 19.22 ? 78   GLN D CB    1 
ATOM   8204  C  CG    . GLN L  3 78  ? 92.481  67.765  132.265 1.00 25.05 ? 78   GLN D CG    1 
ATOM   8205  C  CD    . GLN L  3 78  ? 93.540  68.714  131.740 1.00 32.08 ? 78   GLN D CD    1 
ATOM   8206  O  OE1   . GLN L  3 78  ? 94.552  68.282  131.186 1.00 37.85 ? 78   GLN D OE1   1 
ATOM   8207  N  NE2   . GLN L  3 78  ? 93.321  70.020  131.925 1.00 36.22 ? 78   GLN D NE2   1 
ATOM   8208  N  N     . SER L  3 79  ? 93.185  67.413  128.442 1.00 15.90 ? 79   SER D N     1 
ATOM   8209  C  CA    . SER L  3 79  ? 94.114  68.178  127.592 1.00 17.53 ? 79   SER D CA    1 
ATOM   8210  C  C     . SER L  3 79  ? 93.440  68.909  126.451 1.00 17.39 ? 79   SER D C     1 
ATOM   8211  O  O     . SER L  3 79  ? 93.696  70.093  126.213 1.00 18.62 ? 79   SER D O     1 
ATOM   8212  C  CB    . SER L  3 79  ? 95.192  67.252  127.010 1.00 20.62 ? 79   SER D CB    1 
ATOM   8213  O  OG    . SER L  3 79  ? 96.000  66.719  128.037 1.00 33.20 ? 79   SER D OG    1 
ATOM   8214  N  N     . ALA L  3 80  ? 92.560  68.207  125.751 1.00 14.73 ? 80   ALA D N     1 
ATOM   8215  C  CA    . ALA L  3 80  ? 91.892  68.789  124.606 1.00 15.40 ? 80   ALA D CA    1 
ATOM   8216  C  C     . ALA L  3 80  ? 90.806  69.791  124.964 1.00 17.19 ? 80   ALA D C     1 
ATOM   8217  O  O     . ALA L  3 80  ? 90.736  70.872  124.379 1.00 16.72 ? 80   ALA D O     1 
ATOM   8218  C  CB    . ALA L  3 80  ? 91.342  67.671  123.690 1.00 15.13 ? 80   ALA D CB    1 
ATOM   8219  N  N     . PHE L  3 81  ? 89.978  69.462  125.954 1.00 16.78 ? 81   PHE D N     1 
ATOM   8220  C  CA    . PHE L  3 81  ? 88.903  70.365  126.329 1.00 16.73 ? 81   PHE D CA    1 
ATOM   8221  C  C     . PHE L  3 81  ? 89.419  71.693  126.883 1.00 16.08 ? 81   PHE D C     1 
ATOM   8222  O  O     . PHE L  3 81  ? 88.761  72.722  126.746 1.00 15.51 ? 81   PHE D O     1 
ATOM   8223  C  CB    . PHE L  3 81  ? 87.987  69.661  127.354 1.00 18.48 ? 81   PHE D CB    1 
ATOM   8224  C  CG    . PHE L  3 81  ? 86.717  70.411  127.646 1.00 15.07 ? 81   PHE D CG    1 
ATOM   8225  C  CD1   . PHE L  3 81  ? 85.827  70.679  126.637 1.00 12.55 ? 81   PHE D CD1   1 
ATOM   8226  C  CD2   . PHE L  3 81  ? 86.429  70.843  128.929 1.00 19.83 ? 81   PHE D CD2   1 
ATOM   8227  C  CE1   . PHE L  3 81  ? 84.638  71.369  126.888 1.00 16.60 ? 81   PHE D CE1   1 
ATOM   8228  C  CE2   . PHE L  3 81  ? 85.244  71.538  129.201 1.00 18.21 ? 81   PHE D CE2   1 
ATOM   8229  C  CZ    . PHE L  3 81  ? 84.362  71.804  128.189 1.00 15.86 ? 81   PHE D CZ    1 
ATOM   8230  N  N     . GLU L  3 82  ? 90.595  71.666  127.493 1.00 17.49 ? 82   GLU D N     1 
ATOM   8231  C  CA    . GLU L  3 82  ? 91.199  72.862  128.084 1.00 18.57 ? 82   GLU D CA    1 
ATOM   8232  C  C     . GLU L  3 82  ? 91.444  73.919  127.013 1.00 17.70 ? 82   GLU D C     1 
ATOM   8233  O  O     . GLU L  3 82  ? 91.444  75.125  127.289 1.00 20.40 ? 82   GLU D O     1 
ATOM   8234  C  CB    . GLU L  3 82  ? 92.518  72.476  128.739 1.00 24.42 ? 82   GLU D CB    1 
ATOM   8235  C  CG    . GLU L  3 82  ? 93.245  73.586  129.447 1.00 35.49 ? 82   GLU D CG    1 
ATOM   8236  C  CD    . GLU L  3 82  ? 94.491  73.054  130.137 1.00 42.04 ? 82   GLU D CD    1 
ATOM   8237  O  OE1   . GLU L  3 82  ? 95.406  72.586  129.427 1.00 48.88 ? 82   GLU D OE1   1 
ATOM   8238  O  OE2   . GLU L  3 82  ? 94.549  73.078  131.384 1.00 51.11 ? 82   GLU D OE2   1 
ATOM   8239  N  N     . LYS L  3 83  ? 91.651  73.454  125.793 1.00 15.10 ? 83   LYS D N     1 
ATOM   8240  C  CA    . LYS L  3 83  ? 91.909  74.347  124.661 1.00 14.68 ? 83   LYS D CA    1 
ATOM   8241  C  C     . LYS L  3 83  ? 90.652  75.015  124.104 1.00 17.24 ? 83   LYS D C     1 
ATOM   8242  O  O     . LYS L  3 83  ? 90.740  75.884  123.221 1.00 19.23 ? 83   LYS D O     1 
ATOM   8243  C  CB    . LYS L  3 83  ? 92.639  73.556  123.560 1.00 17.57 ? 83   LYS D CB    1 
ATOM   8244  C  CG    . LYS L  3 83  ? 93.976  73.020  124.084 1.00 23.73 ? 83   LYS D CG    1 
ATOM   8245  C  CD    . LYS L  3 83  ? 94.911  72.497  123.022 1.00 32.68 ? 83   LYS D CD    1 
ATOM   8246  C  CE    . LYS L  3 83  ? 96.288  72.186  123.638 1.00 35.00 ? 83   LYS D CE    1 
ATOM   8247  N  NZ    . LYS L  3 83  ? 96.938  73.417  124.201 1.00 38.49 ? 83   LYS D NZ    1 
ATOM   8248  N  N     . LEU L  3 84  ? 89.482  74.649  124.627 1.00 15.86 ? 84   LEU D N     1 
ATOM   8249  C  CA    . LEU L  3 84  ? 88.229  75.211  124.129 1.00 13.54 ? 84   LEU D CA    1 
ATOM   8250  C  C     . LEU L  3 84  ? 87.588  76.271  125.039 1.00 15.07 ? 84   LEU D C     1 
ATOM   8251  O  O     . LEU L  3 84  ? 86.407  76.575  124.910 1.00 16.29 ? 84   LEU D O     1 
ATOM   8252  C  CB    . LEU L  3 84  ? 87.235  74.063  123.847 1.00 13.09 ? 84   LEU D CB    1 
ATOM   8253  C  CG    . LEU L  3 84  ? 87.752  72.992  122.862 1.00 16.13 ? 84   LEU D CG    1 
ATOM   8254  C  CD1   . LEU L  3 84  ? 86.770  71.802  122.784 1.00 15.79 ? 84   LEU D CD1   1 
ATOM   8255  C  CD2   . LEU L  3 84  ? 87.931  73.625  121.453 1.00 15.92 ? 84   LEU D CD2   1 
ATOM   8256  N  N     . GLN L  3 85  ? 88.388  76.871  125.909 1.00 17.67 ? 85   GLN D N     1 
ATOM   8257  C  CA    . GLN L  3 85  ? 87.887  77.882  126.845 1.00 18.59 ? 85   GLN D CA    1 
ATOM   8258  C  C     . GLN L  3 85  ? 87.159  79.037  126.165 1.00 20.25 ? 85   GLN D C     1 
ATOM   8259  O  O     . GLN L  3 85  ? 86.226  79.614  126.729 1.00 21.25 ? 85   GLN D O     1 
ATOM   8260  C  CB    . GLN L  3 85  ? 89.051  78.411  127.689 1.00 21.15 ? 85   GLN D CB    1 
ATOM   8261  C  CG    . GLN L  3 85  ? 88.663  79.523  128.672 1.00 29.27 ? 85   GLN D CG    1 
ATOM   8262  C  CD    . GLN L  3 85  ? 88.060  79.000  129.975 1.00 32.41 ? 85   GLN D CD    1 
ATOM   8263  O  OE1   . GLN L  3 85  ? 87.491  79.770  130.766 1.00 28.39 ? 85   GLN D OE1   1 
ATOM   8264  N  NE2   . GLN L  3 85  ? 88.203  77.697  130.216 1.00 30.27 ? 85   GLN D NE2   1 
ATOM   8265  N  N     . HIS L  3 86  ? 87.572  79.390  124.947 1.00 19.19 ? 86   HIS D N     1 
ATOM   8266  C  CA    . HIS L  3 86  ? 86.904  80.499  124.248 1.00 17.35 ? 86   HIS D CA    1 
ATOM   8267  C  C     . HIS L  3 86  ? 85.551  80.131  123.670 1.00 18.87 ? 86   HIS D C     1 
ATOM   8268  O  O     . HIS L  3 86  ? 84.749  81.013  123.362 1.00 24.15 ? 86   HIS D O     1 
ATOM   8269  C  CB    . HIS L  3 86  ? 87.800  81.038  123.117 1.00 17.14 ? 86   HIS D CB    1 
ATOM   8270  C  CG    . HIS L  3 86  ? 88.181  79.997  122.111 1.00 18.81 ? 86   HIS D CG    1 
ATOM   8271  N  ND1   . HIS L  3 86  ? 88.884  78.859  122.448 1.00 19.11 ? 86   HIS D ND1   1 
ATOM   8272  C  CD2   . HIS L  3 86  ? 87.939  79.916  120.786 1.00 17.00 ? 86   HIS D CD2   1 
ATOM   8273  C  CE1   . HIS L  3 86  ? 89.064  78.121  121.367 1.00 19.69 ? 86   HIS D CE1   1 
ATOM   8274  N  NE2   . HIS L  3 86  ? 88.496  78.741  120.345 1.00 17.50 ? 86   HIS D NE2   1 
ATOM   8275  N  N     . ILE L  3 87  ? 85.300  78.831  123.522 1.00 17.28 ? 87   ILE D N     1 
ATOM   8276  C  CA    . ILE L  3 87  ? 84.045  78.293  122.986 1.00 19.04 ? 87   ILE D CA    1 
ATOM   8277  C  C     . ILE L  3 87  ? 83.117  77.852  124.133 1.00 17.26 ? 87   ILE D C     1 
ATOM   8278  O  O     . ILE L  3 87  ? 81.892  77.836  123.980 1.00 18.05 ? 87   ILE D O     1 
ATOM   8279  C  CB    . ILE L  3 87  ? 84.325  77.024  122.081 1.00 22.08 ? 87   ILE D CB    1 
ATOM   8280  C  CG1   . ILE L  3 87  ? 85.185  77.442  120.883 1.00 30.69 ? 87   ILE D CG1   1 
ATOM   8281  C  CG2   . ILE L  3 87  ? 83.022  76.373  121.605 1.00 30.50 ? 87   ILE D CG2   1 
ATOM   8282  C  CD1   . ILE L  3 87  ? 84.649  78.625  120.177 1.00 27.01 ? 87   ILE D CD1   1 
ATOM   8283  N  N     . ARG L  3 88  ? 83.716  77.488  125.270 1.00 19.57 ? 88   ARG D N     1 
ATOM   8284  C  CA    . ARG L  3 88  ? 82.950  77.002  126.441 1.00 17.41 ? 88   ARG D CA    1 
ATOM   8285  C  C     . ARG L  3 88  ? 83.774  77.342  127.669 1.00 19.50 ? 88   ARG D C     1 
ATOM   8286  O  O     . ARG L  3 88  ? 84.468  76.481  128.248 1.00 16.62 ? 88   ARG D O     1 
ATOM   8287  C  CB    . ARG L  3 88  ? 82.737  75.475  126.333 1.00 18.34 ? 88   ARG D CB    1 
ATOM   8288  C  CG    . ARG L  3 88  ? 81.662  74.903  127.252 1.00 16.18 ? 88   ARG D CG    1 
ATOM   8289  C  CD    . ARG L  3 88  ? 80.280  75.381  126.794 1.00 17.22 ? 88   ARG D CD    1 
ATOM   8290  N  NE    . ARG L  3 88  ? 79.194  74.528  127.286 1.00 18.00 ? 88   ARG D NE    1 
ATOM   8291  C  CZ    . ARG L  3 88  ? 78.678  74.589  128.517 1.00 17.42 ? 88   ARG D CZ    1 
ATOM   8292  N  NH1   . ARG L  3 88  ? 79.140  75.483  129.396 1.00 15.84 ? 88   ARG D NH1   1 
ATOM   8293  N  NH2   . ARG L  3 88  ? 77.737  73.727  128.886 1.00 18.91 ? 88   ARG D NH2   1 
ATOM   8294  N  N     . PRO L  3 89  ? 83.723  78.619  128.088 1.00 18.02 ? 89   PRO D N     1 
ATOM   8295  C  CA    . PRO L  3 89  ? 84.496  79.046  129.257 1.00 19.03 ? 89   PRO D CA    1 
ATOM   8296  C  C     . PRO L  3 89  ? 83.996  78.493  130.579 1.00 17.89 ? 89   PRO D C     1 
ATOM   8297  O  O     . PRO L  3 89  ? 82.828  78.066  130.704 1.00 19.47 ? 89   PRO D O     1 
ATOM   8298  C  CB    . PRO L  3 89  ? 84.418  80.579  129.190 1.00 20.15 ? 89   PRO D CB    1 
ATOM   8299  C  CG    . PRO L  3 89  ? 83.120  80.844  128.463 1.00 19.99 ? 89   PRO D CG    1 
ATOM   8300  C  CD    . PRO L  3 89  ? 83.095  79.764  127.403 1.00 20.14 ? 89   PRO D CD    1 
ATOM   8301  N  N     . GLY L  3 90  ? 84.896  78.516  131.558 1.00 20.50 ? 90   GLY D N     1 
ATOM   8302  C  CA    . GLY L  3 90  ? 84.558  78.025  132.883 1.00 19.73 ? 90   GLY D CA    1 
ATOM   8303  C  C     . GLY L  3 90  ? 85.751  77.441  133.601 1.00 21.40 ? 90   GLY D C     1 
ATOM   8304  O  O     . GLY L  3 90  ? 86.822  77.285  133.023 1.00 20.01 ? 90   GLY D O     1 
ATOM   8305  N  N     . ASP L  3 91  ? 85.564  77.131  134.878 1.00 19.71 ? 91   ASP D N     1 
ATOM   8306  C  CA    . ASP L  3 91  ? 86.615  76.541  135.701 1.00 19.96 ? 91   ASP D CA    1 
ATOM   8307  C  C     . ASP L  3 91  ? 86.236  75.059  135.728 1.00 21.74 ? 91   ASP D C     1 
ATOM   8308  O  O     . ASP L  3 91  ? 85.432  74.599  136.553 1.00 19.49 ? 91   ASP D O     1 
ATOM   8309  C  CB    . ASP L  3 91  ? 86.570  77.152  137.101 1.00 22.49 ? 91   ASP D CB    1 
ATOM   8310  C  CG    . ASP L  3 91  ? 87.589  76.537  138.041 1.00 27.14 ? 91   ASP D CG    1 
ATOM   8311  O  OD1   . ASP L  3 91  ? 88.429  75.741  137.579 1.00 27.52 ? 91   ASP D OD1   1 
ATOM   8312  O  OD2   . ASP L  3 91  ? 87.544  76.871  139.245 1.00 29.46 ? 91   ASP D OD2   1 
ATOM   8313  N  N     . TRP L  3 92  ? 86.814  74.337  134.775 1.00 18.94 ? 92   TRP D N     1 
ATOM   8314  C  CA    . TRP L  3 92  ? 86.524  72.923  134.557 1.00 21.13 ? 92   TRP D CA    1 
ATOM   8315  C  C     . TRP L  3 92  ? 87.468  71.946  135.232 1.00 20.55 ? 92   TRP D C     1 
ATOM   8316  O  O     . TRP L  3 92  ? 88.667  72.217  135.369 1.00 20.28 ? 92   TRP D O     1 
ATOM   8317  C  CB    . TRP L  3 92  ? 86.531  72.636  133.039 1.00 17.10 ? 92   TRP D CB    1 
ATOM   8318  C  CG    . TRP L  3 92  ? 85.622  73.540  132.241 1.00 18.52 ? 92   TRP D CG    1 
ATOM   8319  C  CD1   . TRP L  3 92  ? 85.982  74.628  131.486 1.00 18.52 ? 92   TRP D CD1   1 
ATOM   8320  C  CD2   . TRP L  3 92  ? 84.208  73.401  132.095 1.00 17.20 ? 92   TRP D CD2   1 
ATOM   8321  N  NE1   . TRP L  3 92  ? 84.873  75.175  130.877 1.00 18.45 ? 92   TRP D NE1   1 
ATOM   8322  C  CE2   . TRP L  3 92  ? 83.766  74.441  131.234 1.00 17.92 ? 92   TRP D CE2   1 
ATOM   8323  C  CE3   . TRP L  3 92  ? 83.266  72.490  132.599 1.00 13.18 ? 92   TRP D CE3   1 
ATOM   8324  C  CZ2   . TRP L  3 92  ? 82.421  74.599  130.863 1.00 15.48 ? 92   TRP D CZ2   1 
ATOM   8325  C  CZ3   . TRP L  3 92  ? 81.924  72.640  132.226 1.00 15.74 ? 92   TRP D CZ3   1 
ATOM   8326  C  CH2   . TRP L  3 92  ? 81.512  73.692  131.362 1.00 16.85 ? 92   TRP D CH2   1 
ATOM   8327  N  N     . ASN L  3 93  ? 86.910  70.810  135.658 1.00 16.86 ? 93   ASN D N     1 
ATOM   8328  C  CA    . ASN L  3 93  ? 87.692  69.744  136.267 1.00 19.16 ? 93   ASN D CA    1 
ATOM   8329  C  C     . ASN L  3 93  ? 87.333  68.425  135.567 1.00 17.36 ? 93   ASN D C     1 
ATOM   8330  O  O     . ASN L  3 93  ? 86.180  68.167  135.283 1.00 18.70 ? 93   ASN D O     1 
ATOM   8331  C  CB    . ASN L  3 93  ? 87.366  69.628  137.763 1.00 24.82 ? 93   ASN D CB    1 
ATOM   8332  C  CG    . ASN L  3 93  ? 88.221  68.584  138.472 1.00 38.94 ? 93   ASN D CG    1 
ATOM   8333  O  OD1   . ASN L  3 93  ? 89.447  68.572  138.327 1.00 44.98 ? 93   ASN D OD1   1 
ATOM   8334  N  ND2   . ASN L  3 93  ? 87.580  67.709  139.254 1.00 45.61 ? 93   ASN D ND2   1 
ATOM   8335  N  N     . VAL L  3 94  ? 88.329  67.606  135.270 1.00 16.44 ? 94   VAL D N     1 
ATOM   8336  C  CA    . VAL L  3 94  ? 88.085  66.309  134.641 1.00 15.20 ? 94   VAL D CA    1 
ATOM   8337  C  C     . VAL L  3 94  ? 88.747  65.298  135.555 1.00 18.88 ? 94   VAL D C     1 
ATOM   8338  O  O     . VAL L  3 94  ? 89.927  65.442  135.884 1.00 20.44 ? 94   VAL D O     1 
ATOM   8339  C  CB    . VAL L  3 94  ? 88.769  66.195  133.256 1.00 16.67 ? 94   VAL D CB    1 
ATOM   8340  C  CG1   . VAL L  3 94  ? 88.465  64.796  132.625 1.00 17.09 ? 94   VAL D CG1   1 
ATOM   8341  C  CG2   . VAL L  3 94  ? 88.259  67.268  132.340 1.00 17.43 ? 94   VAL D CG2   1 
ATOM   8342  N  N     . LYS L  3 95  ? 88.005  64.294  135.994 1.00 17.23 ? 95   LYS D N     1 
ATOM   8343  C  CA    . LYS L  3 95  ? 88.608  63.320  136.873 1.00 20.26 ? 95   LYS D CA    1 
ATOM   8344  C  C     . LYS L  3 95  ? 88.048  61.916  136.763 1.00 17.82 ? 95   LYS D C     1 
ATOM   8345  O  O     . LYS L  3 95  ? 86.849  61.698  136.546 1.00 17.40 ? 95   LYS D O     1 
ATOM   8346  C  CB    . LYS L  3 95  ? 88.523  63.796  138.319 1.00 27.38 ? 95   LYS D CB    1 
ATOM   8347  C  CG    . LYS L  3 95  ? 87.189  63.662  138.967 1.00 33.46 ? 95   LYS D CG    1 
ATOM   8348  C  CD    . LYS L  3 95  ? 87.368  63.873  140.470 1.00 43.06 ? 95   LYS D CD    1 
ATOM   8349  C  CE    . LYS L  3 95  ? 86.043  63.958  141.198 1.00 44.52 ? 95   LYS D CE    1 
ATOM   8350  N  NZ    . LYS L  3 95  ? 86.250  64.313  142.632 1.00 45.67 ? 95   LYS D NZ    1 
ATOM   8351  N  N     . GLN L  3 96  ? 88.957  60.967  136.891 1.00 19.97 ? 96   GLN D N     1 
ATOM   8352  C  CA    . GLN L  3 96  ? 88.613  59.563  136.858 1.00 16.53 ? 96   GLN D CA    1 
ATOM   8353  C  C     . GLN L  3 96  ? 88.126  59.236  138.253 1.00 22.48 ? 96   GLN D C     1 
ATOM   8354  O  O     . GLN L  3 96  ? 88.827  59.517  139.232 1.00 24.61 ? 96   GLN D O     1 
ATOM   8355  C  CB    . GLN L  3 96  ? 89.859  58.746  136.523 1.00 21.04 ? 96   GLN D CB    1 
ATOM   8356  C  CG    . GLN L  3 96  ? 89.621  57.258  136.577 1.00 21.03 ? 96   GLN D CG    1 
ATOM   8357  C  CD    . GLN L  3 96  ? 90.898  56.462  136.440 1.00 19.51 ? 96   GLN D CD    1 
ATOM   8358  O  OE1   . GLN L  3 96  ? 92.010  57.006  136.556 1.00 21.90 ? 96   GLN D OE1   1 
ATOM   8359  N  NE2   . GLN L  3 96  ? 90.758  55.171  136.217 1.00 17.49 ? 96   GLN D NE2   1 
ATOM   8360  N  N     . VAL L  3 97  ? 86.923  58.681  138.364 1.00 20.85 ? 97   VAL D N     1 
ATOM   8361  C  CA    . VAL L  3 97  ? 86.380  58.321  139.668 1.00 26.73 ? 97   VAL D CA    1 
ATOM   8362  C  C     . VAL L  3 97  ? 85.987  56.841  139.722 1.00 30.74 ? 97   VAL D C     1 
ATOM   8363  O  O     . VAL L  3 97  ? 86.727  56.035  140.272 1.00 30.43 ? 97   VAL D O     1 
ATOM   8364  C  CB    . VAL L  3 97  ? 85.155  59.174  140.031 1.00 31.61 ? 97   VAL D CB    1 
ATOM   8365  C  CG1   . VAL L  3 97  ? 84.587  58.686  141.359 1.00 32.06 ? 97   VAL D CG1   1 
ATOM   8366  C  CG2   . VAL L  3 97  ? 85.567  60.654  140.149 1.00 28.42 ? 97   VAL D CG2   1 
ATOM   8367  N  N     . GLY L  3 98  ? 84.831  56.497  139.148 1.00 29.48 ? 98   GLY D N     1 
ATOM   8368  C  CA    . GLY L  3 98  ? 84.380  55.108  139.130 1.00 35.43 ? 98   GLY D CA    1 
ATOM   8369  C  C     . GLY L  3 98  ? 84.147  54.535  140.521 1.00 39.98 ? 98   GLY D C     1 
ATOM   8370  O  O     . GLY L  3 98  ? 83.468  55.152  141.344 1.00 38.57 ? 98   GLY D O     1 
ATOM   8371  N  N     . SER L  3 99  ? 84.712  53.360  140.796 1.00 41.60 ? 99   SER D N     1 
ATOM   8372  C  CA    . SER L  3 99  ? 84.538  52.724  142.101 1.00 44.37 ? 99   SER D CA    1 
ATOM   8373  C  C     . SER L  3 99  ? 85.394  53.291  143.241 1.00 44.58 ? 99   SER D C     1 
ATOM   8374  O  O     . SER L  3 99  ? 85.344  52.784  144.356 1.00 43.43 ? 99   SER D O     1 
ATOM   8375  C  CB    . SER L  3 99  ? 84.776  51.212  141.979 1.00 45.57 ? 99   SER D CB    1 
ATOM   8376  O  OG    . SER L  3 99  ? 86.014  50.933  141.348 1.00 44.82 ? 99   SER D OG    1 
ATOM   8377  N  N     . ARG L  3 100 ? 86.167  54.343  142.985 1.00 47.00 ? 100  ARG D N     1 
ATOM   8378  C  CA    . ARG L  3 100 ? 86.986  54.918  144.053 1.00 46.68 ? 100  ARG D CA    1 
ATOM   8379  C  C     . ARG L  3 100 ? 86.077  55.580  145.070 1.00 47.36 ? 100  ARG D C     1 
ATOM   8380  O  O     . ARG L  3 100 ? 86.509  55.950  146.167 1.00 47.57 ? 100  ARG D O     1 
ATOM   8381  C  CB    . ARG L  3 100 ? 87.997  55.916  143.480 1.00 49.38 ? 100  ARG D CB    1 
ATOM   8382  C  CG    . ARG L  3 100 ? 88.928  55.218  142.513 1.00 51.16 ? 100  ARG D CG    1 
ATOM   8383  C  CD    . ARG L  3 100 ? 90.038  56.073  141.925 1.00 53.66 ? 100  ARG D CD    1 
ATOM   8384  N  NE    . ARG L  3 100 ? 90.799  55.217  141.019 1.00 54.49 ? 100  ARG D NE    1 
ATOM   8385  C  CZ    . ARG L  3 100 ? 91.865  55.582  140.320 1.00 55.85 ? 100  ARG D CZ    1 
ATOM   8386  N  NH1   . ARG L  3 100 ? 92.342  56.820  140.405 1.00 58.37 ? 100  ARG D NH1   1 
ATOM   8387  N  NH2   . ARG L  3 100 ? 92.449  54.698  139.524 1.00 52.01 ? 100  ARG D NH2   1 
ATOM   8388  N  N     . ASN L  3 101 ? 84.804  55.710  144.705 1.00 45.45 ? 101  ASN D N     1 
ATOM   8389  C  CA    . ASN L  3 101 ? 83.830  56.304  145.600 1.00 45.18 ? 101  ASN D CA    1 
ATOM   8390  C  C     . ASN L  3 101 ? 82.408  56.210  145.082 1.00 46.10 ? 101  ASN D C     1 
ATOM   8391  O  O     . ASN L  3 101 ? 82.143  56.434  143.901 1.00 48.05 ? 101  ASN D O     1 
ATOM   8392  C  CB    . ASN L  3 101 ? 84.175  57.769  145.851 1.00 46.36 ? 101  ASN D CB    1 
ATOM   8393  C  CG    . ASN L  3 101 ? 83.254  58.407  146.861 1.00 46.69 ? 101  ASN D CG    1 
ATOM   8394  O  OD1   . ASN L  3 101 ? 82.970  57.820  147.907 1.00 51.15 ? 101  ASN D OD1   1 
ATOM   8395  N  ND2   . ASN L  3 101 ? 82.783  59.613  146.561 1.00 43.91 ? 101  ASN D ND2   1 
ATOM   8396  N  N     . ARG L  3 102 ? 81.479  55.870  145.964 1.00 45.42 ? 102  ARG D N     1 
ATOM   8397  C  CA    . ARG L  3 102 ? 80.098  55.812  145.536 1.00 44.39 ? 102  ARG D CA    1 
ATOM   8398  C  C     . ARG L  3 102 ? 79.427  57.094  146.024 1.00 42.61 ? 102  ARG D C     1 
ATOM   8399  O  O     . ARG L  3 102 ? 79.872  57.709  147.003 1.00 40.65 ? 102  ARG D O     1 
ATOM   8400  C  CB    . ARG L  3 102 ? 79.409  54.559  146.080 1.00 48.59 ? 102  ARG D CB    1 
ATOM   8401  C  CG    . ARG L  3 102 ? 78.510  53.914  145.030 1.00 53.18 ? 102  ARG D CG    1 
ATOM   8402  C  CD    . ARG L  3 102 ? 78.094  52.491  145.366 1.00 57.28 ? 102  ARG D CD    1 
ATOM   8403  N  NE    . ARG L  3 102 ? 77.285  51.910  144.291 1.00 60.04 ? 102  ARG D NE    1 
ATOM   8404  C  CZ    . ARG L  3 102 ? 76.886  50.642  144.259 1.00 60.00 ? 102  ARG D CZ    1 
ATOM   8405  N  NH1   . ARG L  3 102 ? 77.218  49.818  145.241 1.00 60.04 ? 102  ARG D NH1   1 
ATOM   8406  N  NH2   . ARG L  3 102 ? 76.161  50.194  143.244 1.00 60.04 ? 102  ARG D NH2   1 
ATOM   8407  N  N     . LEU L  3 103 ? 78.377  57.506  145.325 1.00 37.82 ? 103  LEU D N     1 
ATOM   8408  C  CA    . LEU L  3 103 ? 77.648  58.722  145.638 1.00 37.22 ? 103  LEU D CA    1 
ATOM   8409  C  C     . LEU L  3 103 ? 78.502  59.972  145.388 1.00 34.27 ? 103  LEU D C     1 
ATOM   8410  O  O     . LEU L  3 103 ? 78.237  61.052  145.923 1.00 32.80 ? 103  LEU D O     1 
ATOM   8411  C  CB    . LEU L  3 103 ? 77.135  58.681  147.086 1.00 40.52 ? 103  LEU D CB    1 
ATOM   8412  C  CG    . LEU L  3 103 ? 75.824  59.426  147.386 1.00 41.52 ? 103  LEU D CG    1 
ATOM   8413  C  CD1   . LEU L  3 103 ? 74.872  59.379  146.188 1.00 42.80 ? 103  LEU D CD1   1 
ATOM   8414  C  CD2   . LEU L  3 103 ? 75.178  58.797  148.618 1.00 45.78 ? 103  LEU D CD2   1 
ATOM   8415  N  N     . GLU L  3 104 ? 79.541  59.819  144.570 1.00 30.93 ? 104  GLU D N     1 
ATOM   8416  C  CA    . GLU L  3 104 ? 80.382  60.953  144.208 1.00 28.75 ? 104  GLU D CA    1 
ATOM   8417  C  C     . GLU L  3 104 ? 79.490  61.976  143.484 1.00 24.59 ? 104  GLU D C     1 
ATOM   8418  O  O     . GLU L  3 104 ? 79.684  63.185  143.624 1.00 25.39 ? 104  GLU D O     1 
ATOM   8419  C  CB    . GLU L  3 104 ? 81.510  60.485  143.278 1.00 30.87 ? 104  GLU D CB    1 
ATOM   8420  C  CG    . GLU L  3 104 ? 82.223  61.575  142.454 1.00 33.92 ? 104  GLU D CG    1 
ATOM   8421  C  CD    . GLU L  3 104 ? 83.217  62.392  143.266 1.00 35.59 ? 104  GLU D CD    1 
ATOM   8422  O  OE1   . GLU L  3 104 ? 83.757  61.847  144.252 1.00 40.69 ? 104  GLU D OE1   1 
ATOM   8423  O  OE2   . GLU L  3 104 ? 83.482  63.566  142.912 1.00 38.74 ? 104  GLU D OE2   1 
ATOM   8424  N  N     . ILE L  3 105 ? 78.502  61.507  142.719 1.00 26.94 ? 105  ILE D N     1 
ATOM   8425  C  CA    . ILE L  3 105 ? 77.668  62.482  142.005 1.00 28.47 ? 105  ILE D CA    1 
ATOM   8426  C  C     . ILE L  3 105 ? 76.804  63.340  142.924 1.00 27.43 ? 105  ILE D C     1 
ATOM   8427  O  O     . ILE L  3 105 ? 76.350  64.410  142.525 1.00 26.79 ? 105  ILE D O     1 
ATOM   8428  C  CB    . ILE L  3 105 ? 76.752  61.852  140.905 1.00 31.34 ? 105  ILE D CB    1 
ATOM   8429  C  CG1   . ILE L  3 105 ? 75.774  60.852  141.505 1.00 32.09 ? 105  ILE D CG1   1 
ATOM   8430  C  CG2   . ILE L  3 105 ? 77.607  61.213  139.813 1.00 33.69 ? 105  ILE D CG2   1 
ATOM   8431  C  CD1   . ILE L  3 105 ? 74.643  60.507  140.540 1.00 36.88 ? 105  ILE D CD1   1 
ATOM   8432  N  N     . ALA L  3 106 ? 76.602  62.891  144.163 1.00 25.37 ? 106  ALA D N     1 
ATOM   8433  C  CA    . ALA L  3 106 ? 75.813  63.677  145.106 1.00 24.69 ? 106  ALA D CA    1 
ATOM   8434  C  C     . ALA L  3 106 ? 76.632  64.880  145.578 1.00 23.87 ? 106  ALA D C     1 
ATOM   8435  O  O     . ALA L  3 106 ? 76.149  65.742  146.309 1.00 22.43 ? 106  ALA D O     1 
ATOM   8436  C  CB    . ALA L  3 106 ? 75.378  62.810  146.282 1.00 24.29 ? 106  ALA D CB    1 
ATOM   8437  N  N     . ARG L  3 107 ? 77.891  64.945  145.150 1.00 23.80 ? 107  ARG D N     1 
ATOM   8438  C  CA    . ARG L  3 107 ? 78.729  66.079  145.478 1.00 24.25 ? 107  ARG D CA    1 
ATOM   8439  C  C     . ARG L  3 107 ? 78.412  67.225  144.514 1.00 22.69 ? 107  ARG D C     1 
ATOM   8440  O  O     . ARG L  3 107 ? 78.866  68.357  144.694 1.00 26.40 ? 107  ARG D O     1 
ATOM   8441  C  CB    . ARG L  3 107 ? 80.206  65.698  145.353 1.00 27.38 ? 107  ARG D CB    1 
ATOM   8442  C  CG    . ARG L  3 107 ? 80.576  64.462  146.179 1.00 31.10 ? 107  ARG D CG    1 
ATOM   8443  C  CD    . ARG L  3 107 ? 82.064  64.188  146.103 1.00 32.11 ? 107  ARG D CD    1 
ATOM   8444  N  NE    . ARG L  3 107 ? 82.840  65.267  146.711 1.00 35.37 ? 107  ARG D NE    1 
ATOM   8445  C  CZ    . ARG L  3 107 ? 84.168  65.285  146.780 1.00 38.16 ? 107  ARG D CZ    1 
ATOM   8446  N  NH1   . ARG L  3 107 ? 84.877  64.284  146.272 1.00 35.89 ? 107  ARG D NH1   1 
ATOM   8447  N  NH2   . ARG L  3 107 ? 84.789  66.300  147.372 1.00 38.65 ? 107  ARG D NH2   1 
ATOM   8448  N  N     . TYR L  3 108 ? 77.615  66.937  143.481 1.00 26.58 ? 108  TYR D N     1 
ATOM   8449  C  CA    . TYR L  3 108 ? 77.280  67.978  142.506 1.00 23.02 ? 108  TYR D CA    1 
ATOM   8450  C  C     . TYR L  3 108 ? 75.821  68.394  142.565 1.00 22.67 ? 108  TYR D C     1 
ATOM   8451  O  O     . TYR L  3 108 ? 74.945  67.605  142.929 1.00 22.16 ? 108  TYR D O     1 
ATOM   8452  C  CB    . TYR L  3 108 ? 77.704  67.523  141.102 1.00 22.83 ? 108  TYR D CB    1 
ATOM   8453  C  CG    . TYR L  3 108 ? 79.154  67.115  141.130 1.00 25.59 ? 108  TYR D CG    1 
ATOM   8454  C  CD1   . TYR L  3 108 ? 79.514  65.781  141.258 1.00 24.03 ? 108  TYR D CD1   1 
ATOM   8455  C  CD2   . TYR L  3 108 ? 80.156  68.079  141.222 1.00 29.06 ? 108  TYR D CD2   1 
ATOM   8456  C  CE1   . TYR L  3 108 ? 80.839  65.404  141.498 1.00 26.10 ? 108  TYR D CE1   1 
ATOM   8457  C  CE2   . TYR L  3 108 ? 81.481  67.718  141.466 1.00 29.77 ? 108  TYR D CE2   1 
ATOM   8458  C  CZ    . TYR L  3 108 ? 81.812  66.386  141.611 1.00 25.87 ? 108  TYR D CZ    1 
ATOM   8459  O  OH    . TYR L  3 108 ? 83.106  66.027  141.927 1.00 32.64 ? 108  TYR D OH    1 
ATOM   8460  N  N     . GLN L  3 109 ? 75.598  69.650  142.199 1.00 23.56 ? 109  GLN D N     1 
ATOM   8461  C  CA    . GLN L  3 109 ? 74.308  70.310  142.270 1.00 22.58 ? 109  GLN D CA    1 
ATOM   8462  C  C     . GLN L  3 109 ? 73.084  69.553  141.778 1.00 20.88 ? 109  GLN D C     1 
ATOM   8463  O  O     . GLN L  3 109 ? 72.108  69.433  142.501 1.00 21.95 ? 109  GLN D O     1 
ATOM   8464  C  CB    . GLN L  3 109 ? 74.399  71.658  141.570 1.00 28.55 ? 109  GLN D CB    1 
ATOM   8465  C  CG    . GLN L  3 109 ? 73.342  72.636  142.009 1.00 35.31 ? 109  GLN D CG    1 
ATOM   8466  C  CD    . GLN L  3 109 ? 73.652  74.069  141.596 1.00 38.43 ? 109  GLN D CD    1 
ATOM   8467  O  OE1   . GLN L  3 109 ? 74.773  74.563  141.761 1.00 37.87 ? 109  GLN D OE1   1 
ATOM   8468  N  NE2   . GLN L  3 109 ? 72.650  74.745  141.071 1.00 40.73 ? 109  GLN D NE2   1 
ATOM   8469  N  N     . GLN L  3 110 ? 73.122  69.011  140.562 1.00 19.03 ? 110  GLN D N     1 
ATOM   8470  C  CA    . GLN L  3 110 ? 71.946  68.316  140.057 1.00 19.26 ? 110  GLN D CA    1 
ATOM   8471  C  C     . GLN L  3 110 ? 71.568  67.031  140.763 1.00 17.34 ? 110  GLN D C     1 
ATOM   8472  O  O     . GLN L  3 110 ? 70.460  66.535  140.574 1.00 17.68 ? 110  GLN D O     1 
ATOM   8473  C  CB    . GLN L  3 110 ? 72.096  67.995  138.557 1.00 18.47 ? 110  GLN D CB    1 
ATOM   8474  C  CG    . GLN L  3 110 ? 72.522  69.161  137.715 1.00 20.10 ? 110  GLN D CG    1 
ATOM   8475  C  CD    . GLN L  3 110 ? 73.982  69.054  137.350 1.00 25.20 ? 110  GLN D CD    1 
ATOM   8476  O  OE1   . GLN L  3 110 ? 74.870  69.160  138.207 1.00 22.76 ? 110  GLN D OE1   1 
ATOM   8477  N  NE2   . GLN L  3 110 ? 74.242  68.806  136.073 1.00 26.25 ? 110  GLN D NE2   1 
ATOM   8478  N  N     . TYR L  3 111 ? 72.464  66.492  141.601 1.00 17.37 ? 111  TYR D N     1 
ATOM   8479  C  CA    . TYR L  3 111 ? 72.193  65.240  142.284 1.00 17.41 ? 111  TYR D CA    1 
ATOM   8480  C  C     . TYR L  3 111 ? 72.449  65.328  143.789 1.00 16.94 ? 111  TYR D C     1 
ATOM   8481  O  O     . TYR L  3 111 ? 72.510  64.307  144.470 1.00 19.65 ? 111  TYR D O     1 
ATOM   8482  C  CB    . TYR L  3 111 ? 73.051  64.112  141.677 1.00 18.40 ? 111  TYR D CB    1 
ATOM   8483  C  CG    . TYR L  3 111 ? 72.790  63.928  140.183 1.00 17.32 ? 111  TYR D CG    1 
ATOM   8484  C  CD1   . TYR L  3 111 ? 73.612  64.534  139.236 1.00 18.75 ? 111  TYR D CD1   1 
ATOM   8485  C  CD2   . TYR L  3 111 ? 71.676  63.223  139.735 1.00 19.63 ? 111  TYR D CD2   1 
ATOM   8486  C  CE1   . TYR L  3 111 ? 73.326  64.454  137.862 1.00 18.04 ? 111  TYR D CE1   1 
ATOM   8487  C  CE2   . TYR L  3 111 ? 71.373  63.132  138.340 1.00 15.67 ? 111  TYR D CE2   1 
ATOM   8488  C  CZ    . TYR L  3 111 ? 72.203  63.755  137.428 1.00 17.10 ? 111  TYR D CZ    1 
ATOM   8489  O  OH    . TYR L  3 111 ? 71.887  63.707  136.074 1.00 15.83 ? 111  TYR D OH    1 
ATOM   8490  N  N     . ALA L  3 112 ? 72.556  66.554  144.286 1.00 20.72 ? 112  ALA D N     1 
ATOM   8491  C  CA    . ALA L  3 112 ? 72.814  66.794  145.710 1.00 22.09 ? 112  ALA D CA    1 
ATOM   8492  C  C     . ALA L  3 112 ? 71.804  66.097  146.619 1.00 23.08 ? 112  ALA D C     1 
ATOM   8493  O  O     . ALA L  3 112 ? 72.139  65.670  147.737 1.00 23.16 ? 112  ALA D O     1 
ATOM   8494  C  CB    . ALA L  3 112 ? 72.806  68.285  145.981 1.00 23.39 ? 112  ALA D CB    1 
ATOM   8495  N  N     . HIS L  3 113 ? 70.563  65.989  146.155 1.00 17.70 ? 113  HIS D N     1 
ATOM   8496  C  CA    . HIS L  3 113 ? 69.498  65.379  146.959 1.00 19.87 ? 113  HIS D CA    1 
ATOM   8497  C  C     . HIS L  3 113 ? 69.632  63.878  147.204 1.00 21.66 ? 113  HIS D C     1 
ATOM   8498  O  O     . HIS L  3 113 ? 68.925  63.325  148.047 1.00 21.79 ? 113  HIS D O     1 
ATOM   8499  C  CB    . HIS L  3 113 ? 68.124  65.663  146.327 1.00 19.27 ? 113  HIS D CB    1 
ATOM   8500  C  CG    . HIS L  3 113 ? 67.998  65.179  144.912 1.00 18.35 ? 113  HIS D CG    1 
ATOM   8501  N  ND1   . HIS L  3 113 ? 68.701  65.744  143.871 1.00 19.70 ? 113  HIS D ND1   1 
ATOM   8502  C  CD2   . HIS L  3 113 ? 67.275  64.166  144.377 1.00 21.97 ? 113  HIS D CD2   1 
ATOM   8503  C  CE1   . HIS L  3 113 ? 68.422  65.094  142.751 1.00 15.99 ? 113  HIS D CE1   1 
ATOM   8504  N  NE2   . HIS L  3 113 ? 67.561  64.131  143.030 1.00 21.02 ? 113  HIS D NE2   1 
ATOM   8505  N  N     . LEU L  3 114 ? 70.526  63.217  146.478 1.00 20.89 ? 114  LEU D N     1 
ATOM   8506  C  CA    . LEU L  3 114 ? 70.674  61.792  146.661 1.00 23.31 ? 114  LEU D CA    1 
ATOM   8507  C  C     . LEU L  3 114 ? 71.247  61.496  148.052 1.00 21.04 ? 114  LEU D C     1 
ATOM   8508  O  O     . LEU L  3 114 ? 71.020  60.423  148.593 1.00 24.22 ? 114  LEU D O     1 
ATOM   8509  C  CB    . LEU L  3 114 ? 71.530  61.191  145.534 1.00 22.47 ? 114  LEU D CB    1 
ATOM   8510  C  CG    . LEU L  3 114 ? 70.950  61.399  144.112 1.00 22.86 ? 114  LEU D CG    1 
ATOM   8511  C  CD1   . LEU L  3 114 ? 71.734  60.569  143.095 1.00 26.36 ? 114  LEU D CD1   1 
ATOM   8512  C  CD2   . LEU L  3 114 ? 69.478  60.973  144.085 1.00 26.26 ? 114  LEU D CD2   1 
ATOM   8513  N  N     . THR L  3 115 ? 71.956  62.462  148.640 1.00 22.55 ? 115  THR D N     1 
ATOM   8514  C  CA    . THR L  3 115 ? 72.483  62.255  149.990 1.00 20.43 ? 115  THR D CA    1 
ATOM   8515  C  C     . THR L  3 115 ? 71.310  62.123  150.960 1.00 20.88 ? 115  THR D C     1 
ATOM   8516  O  O     . THR L  3 115 ? 71.292  61.225  151.812 1.00 24.38 ? 115  THR D O     1 
ATOM   8517  C  CB    . THR L  3 115 ? 73.405  63.425  150.431 1.00 23.39 ? 115  THR D CB    1 
ATOM   8518  O  OG1   . THR L  3 115 ? 74.587  63.412  149.621 1.00 26.82 ? 115  THR D OG1   1 
ATOM   8519  C  CG2   . THR L  3 115 ? 73.813  63.268  151.910 1.00 26.82 ? 115  THR D CG2   1 
ATOM   8520  N  N     . ALA L  3 116 ? 70.329  63.003  150.828 1.00 23.03 ? 116  ALA D N     1 
ATOM   8521  C  CA    . ALA L  3 116 ? 69.145  62.964  151.679 1.00 24.44 ? 116  ALA D CA    1 
ATOM   8522  C  C     . ALA L  3 116 ? 68.353  61.669  151.476 1.00 24.64 ? 116  ALA D C     1 
ATOM   8523  O  O     . ALA L  3 116 ? 67.834  61.101  152.441 1.00 24.87 ? 116  ALA D O     1 
ATOM   8524  C  CB    . ALA L  3 116 ? 68.253  64.181  151.402 1.00 24.34 ? 116  ALA D CB    1 
ATOM   8525  N  N     . LEU L  3 117 ? 68.258  61.187  150.235 1.00 22.45 ? 117  LEU D N     1 
ATOM   8526  C  CA    . LEU L  3 117 ? 67.524  59.950  149.993 1.00 24.20 ? 117  LEU D CA    1 
ATOM   8527  C  C     . LEU L  3 117 ? 68.268  58.792  150.668 1.00 24.12 ? 117  LEU D C     1 
ATOM   8528  O  O     . LEU L  3 117 ? 67.654  57.962  151.343 1.00 25.45 ? 117  LEU D O     1 
ATOM   8529  C  CB    . LEU L  3 117 ? 67.340  59.702  148.482 1.00 29.96 ? 117  LEU D CB    1 
ATOM   8530  C  CG    . LEU L  3 117 ? 66.459  60.764  147.790 1.00 31.86 ? 117  LEU D CG    1 
ATOM   8531  C  CD1   . LEU L  3 117 ? 66.331  60.475  146.300 1.00 34.25 ? 117  LEU D CD1   1 
ATOM   8532  C  CD2   . LEU L  3 117 ? 65.080  60.786  148.433 1.00 36.19 ? 117  LEU D CD2   1 
ATOM   8533  N  N     . ALA L  3 118 ? 69.595  58.768  150.534 1.00 22.05 ? 118  ALA D N     1 
ATOM   8534  C  CA    . ALA L  3 118 ? 70.389  57.710  151.148 1.00 24.47 ? 118  ALA D CA    1 
ATOM   8535  C  C     . ALA L  3 118 ? 70.267  57.762  152.686 1.00 25.94 ? 118  ALA D C     1 
ATOM   8536  O  O     . ALA L  3 118 ? 70.194  56.717  153.332 1.00 25.82 ? 118  ALA D O     1 
ATOM   8537  C  CB    . ALA L  3 118 ? 71.850  57.824  150.710 1.00 24.51 ? 118  ALA D CB    1 
ATOM   8538  N  N     . LYS L  3 119 ? 70.215  58.965  153.261 1.00 23.95 ? 119  LYS D N     1 
ATOM   8539  C  CA    . LYS L  3 119 ? 70.084  59.098  154.717 1.00 28.34 ? 119  LYS D CA    1 
ATOM   8540  C  C     . LYS L  3 119 ? 68.719  58.585  155.148 1.00 28.64 ? 119  LYS D C     1 
ATOM   8541  O  O     . LYS L  3 119 ? 68.605  57.901  156.168 1.00 30.60 ? 119  LYS D O     1 
ATOM   8542  C  CB    . LYS L  3 119 ? 70.241  60.552  155.162 1.00 30.10 ? 119  LYS D CB    1 
ATOM   8543  C  CG    . LYS L  3 119 ? 71.562  61.191  154.770 1.00 35.52 ? 119  LYS D CG    1 
ATOM   8544  C  CD    . LYS L  3 119 ? 72.763  60.658  155.555 1.00 39.94 ? 119  LYS D CD    1 
ATOM   8545  C  CE    . LYS L  3 119 ? 74.040  61.419  155.155 1.00 43.01 ? 119  LYS D CE    1 
ATOM   8546  N  NZ    . LYS L  3 119 ? 75.282  60.858  155.764 1.00 49.59 ? 119  LYS D NZ    1 
ATOM   8547  N  N     . ALA L  3 120 ? 67.689  58.906  154.367 1.00 29.61 ? 120  ALA D N     1 
ATOM   8548  C  CA    . ALA L  3 120 ? 66.334  58.446  154.669 1.00 30.79 ? 120  ALA D CA    1 
ATOM   8549  C  C     . ALA L  3 120 ? 66.263  56.910  154.582 1.00 29.87 ? 120  ALA D C     1 
ATOM   8550  O  O     . ALA L  3 120 ? 65.663  56.268  155.440 1.00 33.06 ? 120  ALA D O     1 
ATOM   8551  C  CB    . ALA L  3 120 ? 65.332  59.075  153.696 1.00 30.91 ? 120  ALA D CB    1 
ATOM   8552  N  N     . ALA L  3 121 ? 66.881  56.325  153.561 1.00 30.26 ? 121  ALA D N     1 
ATOM   8553  C  CA    . ALA L  3 121 ? 66.852  54.871  153.406 1.00 33.05 ? 121  ALA D CA    1 
ATOM   8554  C  C     . ALA L  3 121 ? 67.600  54.217  154.558 1.00 38.05 ? 121  ALA D C     1 
ATOM   8555  O  O     . ALA L  3 121 ? 67.280  53.107  154.984 1.00 41.29 ? 121  ALA D O     1 
ATOM   8556  C  CB    . ALA L  3 121 ? 67.486  54.464  152.077 1.00 32.80 ? 121  ALA D CB    1 
ATOM   8557  N  N     . GLU L  3 122 ? 68.600  54.926  155.059 1.00 39.78 ? 122  GLU D N     1 
ATOM   8558  C  CA    . GLU L  3 122 ? 69.432  54.461  156.149 1.00 45.66 ? 122  GLU D CA    1 
ATOM   8559  C  C     . GLU L  3 122 ? 68.635  54.298  157.437 1.00 47.57 ? 122  GLU D C     1 
ATOM   8560  O  O     . GLU L  3 122 ? 69.002  53.513  158.308 1.00 48.47 ? 122  GLU D O     1 
ATOM   8561  C  CB    . GLU L  3 122 ? 70.556  55.470  156.334 1.00 46.63 ? 122  GLU D CB    1 
ATOM   8562  C  CG    . GLU L  3 122 ? 71.544  55.181  157.396 1.00 52.56 ? 122  GLU D CG    1 
ATOM   8563  C  CD    . GLU L  3 122 ? 72.507  56.335  157.507 1.00 55.45 ? 122  GLU D CD    1 
ATOM   8564  O  OE1   . GLU L  3 122 ? 73.096  56.693  156.465 1.00 57.19 ? 122  GLU D OE1   1 
ATOM   8565  O  OE2   . GLU L  3 122 ? 72.658  56.892  158.616 1.00 58.08 ? 122  GLU D OE2   1 
ATOM   8566  N  N     . GLU L  3 123 ? 67.541  55.037  157.561 1.00 48.33 ? 123  GLU D N     1 
ATOM   8567  C  CA    . GLU L  3 123 ? 66.730  54.931  158.761 1.00 49.95 ? 123  GLU D CA    1 
ATOM   8568  C  C     . GLU L  3 123 ? 65.403  54.224  158.496 1.00 47.79 ? 123  GLU D C     1 
ATOM   8569  O  O     . GLU L  3 123 ? 64.696  53.859  159.432 1.00 47.59 ? 123  GLU D O     1 
ATOM   8570  C  CB    . GLU L  3 123 ? 66.526  56.315  159.373 1.00 52.72 ? 123  GLU D CB    1 
ATOM   8571  C  CG    . GLU L  3 123 ? 67.838  56.928  159.849 1.00 55.92 ? 123  GLU D CG    1 
ATOM   8572  C  CD    . GLU L  3 123 ? 67.640  58.196  160.654 1.00 60.04 ? 123  GLU D CD    1 
ATOM   8573  O  OE1   . GLU L  3 123 ? 67.016  58.120  161.741 1.00 60.04 ? 123  GLU D OE1   1 
ATOM   8574  O  OE2   . GLU L  3 123 ? 68.106  59.270  160.201 1.00 60.04 ? 123  GLU D OE2   1 
ATOM   8575  N  N     . ASN L  3 124 ? 65.064  54.039  157.224 1.00 47.18 ? 124  ASN D N     1 
ATOM   8576  C  CA    . ASN L  3 124 ? 63.857  53.302  156.864 1.00 46.97 ? 124  ASN D CA    1 
ATOM   8577  C  C     . ASN L  3 124 ? 64.153  52.273  155.782 1.00 47.91 ? 124  ASN D C     1 
ATOM   8578  O  O     . ASN L  3 124 ? 64.340  52.609  154.610 1.00 46.85 ? 124  ASN D O     1 
ATOM   8579  C  CB    . ASN L  3 124 ? 62.725  54.194  156.354 1.00 48.36 ? 124  ASN D CB    1 
ATOM   8580  C  CG    . ASN L  3 124 ? 61.575  53.363  155.783 1.00 52.65 ? 124  ASN D CG    1 
ATOM   8581  O  OD1   . ASN L  3 124 ? 61.166  52.363  156.380 1.00 55.12 ? 124  ASN D OD1   1 
ATOM   8582  N  ND2   . ASN L  3 124 ? 61.066  53.758  154.624 1.00 54.81 ? 124  ASN D ND2   1 
ATOM   8583  N  N     . PRO L  3 125 ? 64.147  50.991  156.159 1.00 50.20 ? 125  PRO D N     1 
ATOM   8584  C  CA    . PRO L  3 125 ? 64.429  49.897  155.227 1.00 51.28 ? 125  PRO D CA    1 
ATOM   8585  C  C     . PRO L  3 125 ? 63.727  50.027  153.885 1.00 54.22 ? 125  PRO D C     1 
ATOM   8586  O  O     . PRO L  3 125 ? 64.379  50.228  152.860 1.00 58.19 ? 125  PRO D O     1 
ATOM   8587  C  CB    . PRO L  3 125 ? 63.979  48.663  156.004 1.00 52.97 ? 125  PRO D CB    1 
ATOM   8588  C  CG    . PRO L  3 125 ? 62.863  49.196  156.847 1.00 50.95 ? 125  PRO D CG    1 
ATOM   8589  C  CD    . PRO L  3 125 ? 63.454  50.484  157.354 1.00 49.71 ? 125  PRO D CD    1 
ATOM   8590  N  N     . GLU L  3 126 ? 62.399  49.925  153.902 1.00 53.09 ? 126  GLU D N     1 
ATOM   8591  C  CA    . GLU L  3 126 ? 61.598  50.019  152.685 1.00 55.34 ? 126  GLU D CA    1 
ATOM   8592  C  C     . GLU L  3 126 ? 62.134  50.993  151.670 1.00 55.79 ? 126  GLU D C     1 
ATOM   8593  O  O     . GLU L  3 126 ? 62.451  50.591  150.550 1.00 60.03 ? 126  GLU D O     1 
ATOM   8594  C  CB    . GLU L  3 126 ? 60.150  50.411  152.996 1.00 55.08 ? 126  GLU D CB    1 
ATOM   8595  C  CG    . GLU L  3 126 ? 59.441  51.151  151.837 1.00 56.67 ? 126  GLU D CG    1 
ATOM   8596  C  CD    . GLU L  3 126 ? 59.622  50.480  150.468 1.00 58.16 ? 126  GLU D CD    1 
ATOM   8597  O  OE1   . GLU L  3 126 ? 59.184  49.324  150.286 1.00 54.15 ? 126  GLU D OE1   1 
ATOM   8598  O  OE2   . GLU L  3 126 ? 60.211  51.116  149.567 1.00 59.93 ? 126  GLU D OE2   1 
ATOM   8599  N  N     . LEU L  3 127 ? 62.204  52.273  152.051 1.00 50.79 ? 127  LEU D N     1 
ATOM   8600  C  CA    . LEU L  3 127 ? 62.710  53.295  151.148 1.00 45.10 ? 127  LEU D CA    1 
ATOM   8601  C  C     . LEU L  3 127 ? 63.820  52.676  150.316 1.00 41.81 ? 127  LEU D C     1 
ATOM   8602  O  O     . LEU L  3 127 ? 63.859  52.843  149.104 1.00 42.51 ? 127  LEU D O     1 
ATOM   8603  C  CB    . LEU L  3 127 ? 63.256  54.494  151.926 1.00 46.60 ? 127  LEU D CB    1 
ATOM   8604  C  CG    . LEU L  3 127 ? 62.248  55.257  152.784 1.00 48.73 ? 127  LEU D CG    1 
ATOM   8605  C  CD1   . LEU L  3 127 ? 62.964  56.314  153.609 1.00 51.58 ? 127  LEU D CD1   1 
ATOM   8606  C  CD2   . LEU L  3 127 ? 61.201  55.889  151.896 1.00 51.06 ? 127  LEU D CD2   1 
ATOM   8607  N  N     . ALA L  3 128 ? 64.705  51.939  150.985 1.00 38.59 ? 128  ALA D N     1 
ATOM   8608  C  CA    . ALA L  3 128 ? 65.827  51.294  150.327 1.00 38.04 ? 128  ALA D CA    1 
ATOM   8609  C  C     . ALA L  3 128 ? 65.384  50.312  149.239 1.00 35.95 ? 128  ALA D C     1 
ATOM   8610  O  O     . ALA L  3 128 ? 65.975  50.264  148.162 1.00 38.00 ? 128  ALA D O     1 
ATOM   8611  C  CB    . ALA L  3 128 ? 66.705  50.578  151.380 1.00 38.85 ? 128  ALA D CB    1 
ATOM   8612  N  N     . ALA L  3 129 ? 64.342  49.531  149.520 1.00 32.67 ? 129  ALA D N     1 
ATOM   8613  C  CA    . ALA L  3 129 ? 63.837  48.556  148.557 1.00 30.57 ? 129  ALA D CA    1 
ATOM   8614  C  C     . ALA L  3 129 ? 63.198  49.241  147.338 1.00 31.44 ? 129  ALA D C     1 
ATOM   8615  O  O     . ALA L  3 129 ? 63.312  48.758  146.201 1.00 28.25 ? 129  ALA D O     1 
ATOM   8616  C  CB    . ALA L  3 129 ? 62.828  47.636  149.242 1.00 27.96 ? 129  ALA D CB    1 
ATOM   8617  N  N     . ALA L  3 130 ? 62.527  50.367  147.575 1.00 29.68 ? 130  ALA D N     1 
ATOM   8618  C  CA    . ALA L  3 130 ? 61.890  51.103  146.486 1.00 30.98 ? 130  ALA D CA    1 
ATOM   8619  C  C     . ALA L  3 130 ? 62.860  52.037  145.772 1.00 29.20 ? 130  ALA D C     1 
ATOM   8620  O  O     . ALA L  3 130 ? 62.925  52.056  144.541 1.00 31.28 ? 130  ALA D O     1 
ATOM   8621  C  CB    . ALA L  3 130 ? 60.707  51.900  147.017 1.00 30.00 ? 130  ALA D CB    1 
ATOM   8622  N  N     . LEU L  3 131 ? 63.628  52.811  146.532 1.00 31.08 ? 131  LEU D N     1 
ATOM   8623  C  CA    . LEU L  3 131 ? 64.559  53.758  145.916 1.00 33.08 ? 131  LEU D CA    1 
ATOM   8624  C  C     . LEU L  3 131 ? 65.719  53.053  145.222 1.00 37.04 ? 131  LEU D C     1 
ATOM   8625  O  O     . LEU L  3 131 ? 66.239  53.546  144.219 1.00 38.19 ? 131  LEU D O     1 
ATOM   8626  C  CB    . LEU L  3 131 ? 65.117  54.729  146.965 1.00 37.67 ? 131  LEU D CB    1 
ATOM   8627  C  CG    . LEU L  3 131 ? 64.107  55.455  147.871 1.00 41.50 ? 131  LEU D CG    1 
ATOM   8628  C  CD1   . LEU L  3 131 ? 64.863  56.221  148.946 1.00 42.03 ? 131  LEU D CD1   1 
ATOM   8629  C  CD2   . LEU L  3 131 ? 63.232  56.394  147.047 1.00 42.50 ? 131  LEU D CD2   1 
ATOM   8630  N  N     . GLY L  3 132 ? 66.130  51.908  145.759 1.00 36.52 ? 132  GLY D N     1 
ATOM   8631  C  CA    . GLY L  3 132 ? 67.239  51.188  145.161 1.00 37.75 ? 132  GLY D CA    1 
ATOM   8632  C  C     . GLY L  3 132 ? 68.559  51.668  145.730 1.00 35.40 ? 132  GLY D C     1 
ATOM   8633  O  O     . GLY L  3 132 ? 68.583  52.394  146.724 1.00 35.94 ? 132  GLY D O     1 
ATOM   8634  N  N     . SER L  3 133 ? 69.660  51.273  145.097 1.00 35.80 ? 133  SER D N     1 
ATOM   8635  C  CA    . SER L  3 133 ? 70.985  51.661  145.560 1.00 37.25 ? 133  SER D CA    1 
ATOM   8636  C  C     . SER L  3 133 ? 71.875  52.063  144.406 1.00 36.26 ? 133  SER D C     1 
ATOM   8637  O  O     . SER L  3 133 ? 72.916  52.694  144.605 1.00 38.36 ? 133  SER D O     1 
ATOM   8638  C  CB    . SER L  3 133 ? 71.658  50.500  146.302 1.00 40.71 ? 133  SER D CB    1 
ATOM   8639  O  OG    . SER L  3 133 ? 71.948  49.430  145.406 1.00 45.17 ? 133  SER D OG    1 
ATOM   8640  N  N     . ASP L  3 134 ? 71.478  51.708  143.191 1.00 36.46 ? 134  ASP D N     1 
ATOM   8641  C  CA    . ASP L  3 134 ? 72.334  52.023  142.053 1.00 32.18 ? 134  ASP D CA    1 
ATOM   8642  C  C     . ASP L  3 134 ? 72.444  53.505  141.708 1.00 31.62 ? 134  ASP D C     1 
ATOM   8643  O  O     . ASP L  3 134 ? 73.326  53.901  140.957 1.00 30.09 ? 134  ASP D O     1 
ATOM   8644  C  CB    . ASP L  3 134 ? 71.921  51.174  140.835 1.00 37.05 ? 134  ASP D CB    1 
ATOM   8645  C  CG    . ASP L  3 134 ? 72.144  49.649  141.071 1.00 38.16 ? 134  ASP D CG    1 
ATOM   8646  O  OD1   . ASP L  3 134 ? 72.998  49.273  141.900 1.00 45.36 ? 134  ASP D OD1   1 
ATOM   8647  O  OD2   . ASP L  3 134 ? 71.472  48.829  140.423 1.00 43.74 ? 134  ASP D OD2   1 
ATOM   8648  N  N     . TYR L  3 135 ? 71.576  54.345  142.264 1.00 31.97 ? 135  TYR D N     1 
ATOM   8649  C  CA    . TYR L  3 135 ? 71.680  55.773  141.978 1.00 31.82 ? 135  TYR D CA    1 
ATOM   8650  C  C     . TYR L  3 135 ? 72.980  56.307  142.586 1.00 34.32 ? 135  TYR D C     1 
ATOM   8651  O  O     . TYR L  3 135 ? 73.401  57.437  142.295 1.00 34.65 ? 135  TYR D O     1 
ATOM   8652  C  CB    . TYR L  3 135 ? 70.449  56.537  142.522 1.00 31.96 ? 135  TYR D CB    1 
ATOM   8653  C  CG    . TYR L  3 135 ? 70.216  56.466  144.016 1.00 33.09 ? 135  TYR D CG    1 
ATOM   8654  C  CD1   . TYR L  3 135 ? 70.920  57.295  144.902 1.00 35.25 ? 135  TYR D CD1   1 
ATOM   8655  C  CD2   . TYR L  3 135 ? 69.281  55.580  144.551 1.00 36.69 ? 135  TYR D CD2   1 
ATOM   8656  C  CE1   . TYR L  3 135 ? 70.694  57.244  146.283 1.00 37.41 ? 135  TYR D CE1   1 
ATOM   8657  C  CE2   . TYR L  3 135 ? 69.048  55.521  145.935 1.00 38.31 ? 135  TYR D CE2   1 
ATOM   8658  C  CZ    . TYR L  3 135 ? 69.758  56.357  146.789 1.00 37.44 ? 135  TYR D CZ    1 
ATOM   8659  O  OH    . TYR L  3 135 ? 69.523  56.311  148.146 1.00 39.98 ? 135  TYR D OH    1 
ATOM   8660  N  N     . THR L  3 136 ? 73.636  55.470  143.397 1.00 32.87 ? 136  THR D N     1 
ATOM   8661  C  CA    . THR L  3 136 ? 74.895  55.844  144.049 1.00 34.65 ? 136  THR D CA    1 
ATOM   8662  C  C     . THR L  3 136 ? 76.120  55.507  143.195 1.00 35.63 ? 136  THR D C     1 
ATOM   8663  O  O     . THR L  3 136 ? 77.247  55.843  143.572 1.00 35.56 ? 136  THR D O     1 
ATOM   8664  C  CB    . THR L  3 136 ? 75.083  55.109  145.398 1.00 31.37 ? 136  THR D CB    1 
ATOM   8665  O  OG1   . THR L  3 136 ? 75.193  53.694  145.164 1.00 36.73 ? 136  THR D OG1   1 
ATOM   8666  C  CG2   . THR L  3 136 ? 73.899  55.381  146.323 1.00 37.42 ? 136  THR D CG2   1 
ATOM   8667  N  N     . ILE L  3 137 ? 75.906  54.844  142.059 1.00 32.82 ? 137  ILE D N     1 
ATOM   8668  C  CA    . ILE L  3 137 ? 77.026  54.445  141.203 1.00 34.05 ? 137  ILE D CA    1 
ATOM   8669  C  C     . ILE L  3 137 ? 77.643  55.611  140.447 1.00 34.62 ? 137  ILE D C     1 
ATOM   8670  O  O     . ILE L  3 137 ? 76.959  56.345  139.734 1.00 33.79 ? 137  ILE D O     1 
ATOM   8671  C  CB    . ILE L  3 137 ? 76.602  53.340  140.194 1.00 35.91 ? 137  ILE D CB    1 
ATOM   8672  C  CG1   . ILE L  3 137 ? 76.164  52.094  140.978 1.00 34.68 ? 137  ILE D CG1   1 
ATOM   8673  C  CG2   . ILE L  3 137 ? 77.764  53.021  139.225 1.00 36.18 ? 137  ILE D CG2   1 
ATOM   8674  C  CD1   . ILE L  3 137 ? 75.719  50.931  140.118 1.00 36.43 ? 137  ILE D CD1   1 
ATOM   8675  N  N     . THR L  3 138 ? 78.954  55.761  140.600 1.00 32.54 ? 138  THR D N     1 
ATOM   8676  C  CA    . THR L  3 138 ? 79.655  56.859  139.978 1.00 30.17 ? 138  THR D CA    1 
ATOM   8677  C  C     . THR L  3 138 ? 80.186  56.555  138.570 1.00 25.08 ? 138  THR D C     1 
ATOM   8678  O  O     . THR L  3 138 ? 80.627  55.453  138.280 1.00 24.70 ? 138  THR D O     1 
ATOM   8679  C  CB    . THR L  3 138 ? 80.811  57.316  140.902 1.00 33.45 ? 138  THR D CB    1 
ATOM   8680  O  OG1   . THR L  3 138 ? 80.260  57.668  142.189 1.00 38.71 ? 138  THR D OG1   1 
ATOM   8681  C  CG2   . THR L  3 138 ? 81.525  58.527  140.323 1.00 34.51 ? 138  THR D CG2   1 
ATOM   8682  N  N     . PRO L  3 139 ? 80.111  57.547  137.683 1.00 21.15 ? 139  PRO D N     1 
ATOM   8683  C  CA    . PRO L  3 139 ? 80.586  57.419  136.300 1.00 21.08 ? 139  PRO D CA    1 
ATOM   8684  C  C     . PRO L  3 139 ? 82.090  57.155  136.342 1.00 18.90 ? 139  PRO D C     1 
ATOM   8685  O  O     . PRO L  3 139 ? 82.751  57.498  137.320 1.00 22.44 ? 139  PRO D O     1 
ATOM   8686  C  CB    . PRO L  3 139 ? 80.279  58.792  135.699 1.00 20.29 ? 139  PRO D CB    1 
ATOM   8687  C  CG    . PRO L  3 139 ? 79.043  59.231  136.513 1.00 20.44 ? 139  PRO D CG    1 
ATOM   8688  C  CD    . PRO L  3 139 ? 79.439  58.839  137.898 1.00 21.54 ? 139  PRO D CD    1 
ATOM   8689  N  N     . ASP L  3 140 ? 82.620  56.516  135.304 1.00 14.42 ? 140  ASP D N     1 
ATOM   8690  C  CA    . ASP L  3 140 ? 84.039  56.252  135.220 1.00 14.80 ? 140  ASP D CA    1 
ATOM   8691  C  C     . ASP L  3 140 ? 84.844  57.541  135.272 1.00 16.15 ? 140  ASP D C     1 
ATOM   8692  O  O     . ASP L  3 140 ? 85.855  57.639  135.978 1.00 16.36 ? 140  ASP D O     1 
ATOM   8693  C  CB    . ASP L  3 140 ? 84.365  55.521  133.920 1.00 14.82 ? 140  ASP D CB    1 
ATOM   8694  C  CG    . ASP L  3 140 ? 83.749  54.152  133.866 1.00 19.82 ? 140  ASP D CG    1 
ATOM   8695  O  OD1   . ASP L  3 140 ? 83.305  53.663  134.923 1.00 14.77 ? 140  ASP D OD1   1 
ATOM   8696  O  OD2   . ASP L  3 140 ? 83.717  53.548  132.780 1.00 14.88 ? 140  ASP D OD2   1 
ATOM   8697  N  N     . ILE L  3 141 ? 84.416  58.522  134.479 1.00 13.72 ? 141  ILE D N     1 
ATOM   8698  C  CA    . ILE L  3 141 ? 85.090  59.811  134.444 1.00 14.70 ? 141  ILE D CA    1 
ATOM   8699  C  C     . ILE L  3 141 ? 84.002  60.877  134.520 1.00 14.08 ? 141  ILE D C     1 
ATOM   8700  O  O     . ILE L  3 141 ? 82.940  60.730  133.906 1.00 14.53 ? 141  ILE D O     1 
ATOM   8701  C  CB    . ILE L  3 141 ? 85.841  60.012  133.085 1.00 13.72 ? 141  ILE D CB    1 
ATOM   8702  C  CG1   . ILE L  3 141 ? 86.929  58.941  132.894 1.00 15.21 ? 141  ILE D CG1   1 
ATOM   8703  C  CG2   . ILE L  3 141 ? 86.442  61.419  133.022 1.00 17.02 ? 141  ILE D CG2   1 
ATOM   8704  C  CD1   . ILE L  3 141 ? 87.473  58.923  131.423 1.00 16.34 ? 141  ILE D CD1   1 
ATOM   8705  N  N     . ILE L  3 142 ? 84.241  61.951  135.274 1.00 13.40 ? 142  ILE D N     1 
ATOM   8706  C  CA    . ILE L  3 142 ? 83.282  63.047  135.302 1.00 13.25 ? 142  ILE D CA    1 
ATOM   8707  C  C     . ILE L  3 142 ? 83.971  64.351  134.909 1.00 15.48 ? 142  ILE D C     1 
ATOM   8708  O  O     . ILE L  3 142 ? 85.187  64.500  135.064 1.00 15.92 ? 142  ILE D O     1 
ATOM   8709  C  CB    . ILE L  3 142 ? 82.631  63.250  136.696 1.00 17.79 ? 142  ILE D CB    1 
ATOM   8710  C  CG1   . ILE L  3 142 ? 83.710  63.487  137.765 1.00 20.80 ? 142  ILE D CG1   1 
ATOM   8711  C  CG2   . ILE L  3 142 ? 81.738  62.054  137.015 1.00 17.59 ? 142  ILE D CG2   1 
ATOM   8712  C  CD1   . ILE L  3 142 ? 83.153  63.833  139.151 1.00 24.48 ? 142  ILE D CD1   1 
ATOM   8713  N  N     . VAL L  3 143 ? 83.207  65.267  134.326 1.00 13.63 ? 143  VAL D N     1 
ATOM   8714  C  CA    . VAL L  3 143 ? 83.727  66.591  134.019 1.00 15.73 ? 143  VAL D CA    1 
ATOM   8715  C  C     . VAL L  3 143 ? 82.801  67.469  134.846 1.00 13.37 ? 143  VAL D C     1 
ATOM   8716  O  O     . VAL L  3 143 ? 81.587  67.288  134.799 1.00 14.16 ? 143  VAL D O     1 
ATOM   8717  C  CB    . VAL L  3 143 ? 83.578  66.968  132.541 1.00 14.48 ? 143  VAL D CB    1 
ATOM   8718  C  CG1   . VAL L  3 143 ? 84.125  68.371  132.320 1.00 15.10 ? 143  VAL D CG1   1 
ATOM   8719  C  CG2   . VAL L  3 143 ? 84.378  65.994  131.667 1.00 15.09 ? 143  VAL D CG2   1 
ATOM   8720  N  N     . THR L  3 144 ? 83.369  68.393  135.623 1.00 15.25 ? 144  THR D N     1 
ATOM   8721  C  CA    . THR L  3 144 ? 82.556  69.268  136.456 1.00 16.00 ? 144  THR D CA    1 
ATOM   8722  C  C     . THR L  3 144 ? 82.915  70.723  136.211 1.00 15.30 ? 144  THR D C     1 
ATOM   8723  O  O     . THR L  3 144 ? 83.998  71.021  135.681 1.00 15.23 ? 144  THR D O     1 
ATOM   8724  C  CB    . THR L  3 144 ? 82.769  68.970  137.953 1.00 16.79 ? 144  THR D CB    1 
ATOM   8725  O  OG1   . THR L  3 144 ? 84.132  69.247  138.302 1.00 21.62 ? 144  THR D OG1   1 
ATOM   8726  C  CG2   . THR L  3 144 ? 82.483  67.506  138.253 1.00 22.65 ? 144  THR D CG2   1 
ATOM   8727  N  N     . ARG L  3 145 ? 82.002  71.621  136.594 1.00 16.72 ? 145  ARG D N     1 
ATOM   8728  C  CA    . ARG L  3 145 ? 82.226  73.063  136.440 1.00 20.02 ? 145  ARG D CA    1 
ATOM   8729  C  C     . ARG L  3 145 ? 82.094  73.737  137.804 1.00 19.09 ? 145  ARG D C     1 
ATOM   8730  O  O     . ARG L  3 145 ? 81.083  73.565  138.486 1.00 21.37 ? 145  ARG D O     1 
ATOM   8731  C  CB    . ARG L  3 145 ? 81.173  73.685  135.511 1.00 19.78 ? 145  ARG D CB    1 
ATOM   8732  C  CG    . ARG L  3 145 ? 81.466  75.146  135.142 1.00 24.15 ? 145  ARG D CG    1 
ATOM   8733  C  CD    . ARG L  3 145 ? 80.357  75.778  134.326 1.00 22.41 ? 145  ARG D CD    1 
ATOM   8734  N  NE    . ARG L  3 145 ? 80.734  77.137  133.951 1.00 20.02 ? 145  ARG D NE    1 
ATOM   8735  C  CZ    . ARG L  3 145 ? 80.114  77.876  133.043 1.00 18.60 ? 145  ARG D CZ    1 
ATOM   8736  N  NH1   . ARG L  3 145 ? 79.074  77.390  132.388 1.00 20.45 ? 145  ARG D NH1   1 
ATOM   8737  N  NH2   . ARG L  3 145 ? 80.519  79.124  132.809 1.00 22.88 ? 145  ARG D NH2   1 
ATOM   8738  N  N     . ASN L  3 146 ? 83.099  74.513  138.181 1.00 20.04 ? 146  ASN D N     1 
ATOM   8739  C  CA    . ASN L  3 146 ? 83.020  75.225  139.451 1.00 22.04 ? 146  ASN D CA    1 
ATOM   8740  C  C     . ASN L  3 146 ? 82.128  76.448  139.260 1.00 22.48 ? 146  ASN D C     1 
ATOM   8741  O  O     . ASN L  3 146 ? 81.950  76.937  138.141 1.00 22.44 ? 146  ASN D O     1 
ATOM   8742  C  CB    . ASN L  3 146 ? 84.410  75.633  139.916 1.00 23.40 ? 146  ASN D CB    1 
ATOM   8743  C  CG    . ASN L  3 146 ? 85.177  74.476  140.516 1.00 31.89 ? 146  ASN D CG    1 
ATOM   8744  O  OD1   . ASN L  3 146 ? 84.595  73.443  140.900 1.00 31.25 ? 146  ASN D OD1   1 
ATOM   8745  N  ND2   . ASN L  3 146 ? 86.483  74.641  140.631 1.00 35.11 ? 146  ASN D ND2   1 
ATOM   8746  N  N     . LEU L  3 147 ? 81.561  76.941  140.360 1.00 23.30 ? 147  LEU D N     1 
ATOM   8747  C  CA    . LEU L  3 147 ? 80.649  78.075  140.292 1.00 23.22 ? 147  LEU D CA    1 
ATOM   8748  C  C     . LEU L  3 147 ? 81.370  79.403  140.064 1.00 25.74 ? 147  LEU D C     1 
ATOM   8749  O  O     . LEU L  3 147 ? 82.589  79.489  140.222 1.00 29.26 ? 147  LEU D O     1 
ATOM   8750  C  CB    . LEU L  3 147 ? 79.774  78.089  141.551 1.00 26.12 ? 147  LEU D CB    1 
ATOM   8751  C  CG    . LEU L  3 147 ? 79.148  76.724  141.863 1.00 27.58 ? 147  LEU D CG    1 
ATOM   8752  C  CD1   . LEU L  3 147 ? 78.194  76.865  143.040 1.00 27.06 ? 147  LEU D CD1   1 
ATOM   8753  C  CD2   . LEU L  3 147 ? 78.401  76.163  140.636 1.00 27.82 ? 147  LEU D CD2   1 
ATOM   8754  N  N     . ILE L  3 148 ? 80.602  80.432  139.707 1.00 26.96 ? 148  ILE D N     1 
ATOM   8755  C  CA    . ILE L  3 148 ? 81.122  81.751  139.341 1.00 27.01 ? 148  ILE D CA    1 
ATOM   8756  C  C     . ILE L  3 148 ? 80.818  82.898  140.309 1.00 27.90 ? 148  ILE D C     1 
ATOM   8757  O  O     . ILE L  3 148 ? 79.700  83.030  140.791 1.00 27.91 ? 148  ILE D O     1 
ATOM   8758  C  CB    . ILE L  3 148 ? 80.543  82.158  137.979 1.00 26.06 ? 148  ILE D CB    1 
ATOM   8759  C  CG1   . ILE L  3 148 ? 80.694  80.992  136.988 1.00 31.07 ? 148  ILE D CG1   1 
ATOM   8760  C  CG2   . ILE L  3 148 ? 81.243  83.383  137.454 1.00 29.62 ? 148  ILE D CG2   1 
ATOM   8761  C  CD1   . ILE L  3 148 ? 80.035  81.258  135.639 1.00 30.24 ? 148  ILE D CD1   1 
ATOM   8762  N  N     . ALA L  3 149 ? 81.816  83.746  140.534 1.00 27.17 ? 149  ALA D N     1 
ATOM   8763  C  CA    . ALA L  3 149 ? 81.663  84.886  141.429 1.00 28.79 ? 149  ALA D CA    1 
ATOM   8764  C  C     . ALA L  3 149 ? 80.911  86.012  140.731 1.00 26.47 ? 149  ALA D C     1 
ATOM   8765  O  O     . ALA L  3 149 ? 80.912  86.098  139.509 1.00 27.82 ? 149  ALA D O     1 
ATOM   8766  C  CB    . ALA L  3 149 ? 83.044  85.380  141.875 1.00 29.16 ? 149  ALA D CB    1 
ATOM   8767  N  N     . ASP L  3 150 ? 80.272  86.877  141.513 1.00 26.43 ? 150  ASP D N     1 
ATOM   8768  C  CA    . ASP L  3 150 ? 79.538  88.008  140.932 1.00 28.26 ? 150  ASP D CA    1 
ATOM   8769  C  C     . ASP L  3 150 ? 80.459  88.866  140.075 1.00 26.24 ? 150  ASP D C     1 
ATOM   8770  O  O     . ASP L  3 150 ? 80.033  89.432  139.074 1.00 26.81 ? 150  ASP D O     1 
ATOM   8771  C  CB    . ASP L  3 150 ? 78.931  88.891  142.034 1.00 32.50 ? 150  ASP D CB    1 
ATOM   8772  C  CG    . ASP L  3 150 ? 77.690  88.280  142.674 1.00 36.88 ? 150  ASP D CG    1 
ATOM   8773  O  OD1   . ASP L  3 150 ? 77.243  87.202  142.233 1.00 34.64 ? 150  ASP D OD1   1 
ATOM   8774  O  OD2   . ASP L  3 150 ? 77.156  88.894  143.627 1.00 40.80 ? 150  ASP D OD2   1 
ATOM   8775  N  N     . ALA L  3 151 ? 81.725  88.970  140.470 1.00 27.50 ? 151  ALA D N     1 
ATOM   8776  C  CA    . ALA L  3 151 ? 82.669  89.783  139.707 1.00 29.90 ? 151  ALA D CA    1 
ATOM   8777  C  C     . ALA L  3 151 ? 82.782  89.337  138.245 1.00 30.00 ? 151  ALA D C     1 
ATOM   8778  O  O     . ALA L  3 151 ? 82.935  90.175  137.350 1.00 29.46 ? 151  ALA D O     1 
ATOM   8779  C  CB    . ALA L  3 151 ? 84.041  89.762  140.376 1.00 29.37 ? 151  ALA D CB    1 
ATOM   8780  N  N     . GLU L  3 152 ? 82.682  88.029  138.009 1.00 29.09 ? 152  GLU D N     1 
ATOM   8781  C  CA    . GLU L  3 152 ? 82.764  87.477  136.644 1.00 28.08 ? 152  GLU D CA    1 
ATOM   8782  C  C     . GLU L  3 152 ? 81.428  87.655  135.891 1.00 25.75 ? 152  GLU D C     1 
ATOM   8783  O  O     . GLU L  3 152 ? 81.400  88.057  134.719 1.00 25.88 ? 152  GLU D O     1 
ATOM   8784  C  CB    . GLU L  3 152 ? 83.140  85.993  136.719 1.00 28.39 ? 152  GLU D CB    1 
ATOM   8785  C  CG    . GLU L  3 152 ? 83.162  85.263  135.372 1.00 31.37 ? 152  GLU D CG    1 
ATOM   8786  C  CD    . GLU L  3 152 ? 84.061  85.938  134.353 1.00 41.89 ? 152  GLU D CD    1 
ATOM   8787  O  OE1   . GLU L  3 152 ? 85.095  86.523  134.762 1.00 43.24 ? 152  GLU D OE1   1 
ATOM   8788  O  OE2   . GLU L  3 152 ? 83.743  85.881  133.141 1.00 43.57 ? 152  GLU D OE2   1 
ATOM   8789  N  N     . ILE L  3 153 ? 80.323  87.357  136.560 1.00 23.98 ? 153  ILE D N     1 
ATOM   8790  C  CA    . ILE L  3 153 ? 79.022  87.543  135.915 1.00 25.06 ? 153  ILE D CA    1 
ATOM   8791  C  C     . ILE L  3 153 ? 78.931  89.022  135.504 1.00 25.75 ? 153  ILE D C     1 
ATOM   8792  O  O     . ILE L  3 153 ? 78.517  89.345  134.388 1.00 22.20 ? 153  ILE D O     1 
ATOM   8793  C  CB    . ILE L  3 153 ? 77.844  87.166  136.874 1.00 25.28 ? 153  ILE D CB    1 
ATOM   8794  C  CG1   . ILE L  3 153 ? 77.856  85.648  137.133 1.00 27.01 ? 153  ILE D CG1   1 
ATOM   8795  C  CG2   . ILE L  3 153 ? 76.490  87.609  136.289 1.00 23.16 ? 153  ILE D CG2   1 
ATOM   8796  C  CD1   . ILE L  3 153 ? 76.865  85.174  138.213 1.00 29.02 ? 153  ILE D CD1   1 
ATOM   8797  N  N     . ASN L  3 154 ? 79.361  89.914  136.403 1.00 26.44 ? 154  ASN D N     1 
ATOM   8798  C  CA    . ASN L  3 154 ? 79.314  91.360  136.159 1.00 25.00 ? 154  ASN D CA    1 
ATOM   8799  C  C     . ASN L  3 154 ? 80.606  91.882  135.548 1.00 28.68 ? 154  ASN D C     1 
ATOM   8800  O  O     . ASN L  3 154 ? 80.965  93.044  135.739 1.00 27.15 ? 154  ASN D O     1 
ATOM   8801  C  CB    . ASN L  3 154 ? 79.086  92.121  137.476 1.00 25.31 ? 154  ASN D CB    1 
ATOM   8802  C  CG    . ASN L  3 154 ? 77.747  91.809  138.120 1.00 24.40 ? 154  ASN D CG    1 
ATOM   8803  O  OD1   . ASN L  3 154 ? 76.794  91.416  137.446 1.00 26.35 ? 154  ASN D OD1   1 
ATOM   8804  N  ND2   . ASN L  3 154 ? 77.661  92.001  139.436 1.00 26.36 ? 154  ASN D ND2   1 
ATOM   8805  N  N     . ARG L  3 155 ? 81.315  91.033  134.820 1.00 27.31 ? 155  ARG D N     1 
ATOM   8806  C  CA    . ARG L  3 155 ? 82.575  91.448  134.223 1.00 30.32 ? 155  ARG D CA    1 
ATOM   8807  C  C     . ARG L  3 155 ? 82.445  92.676  133.327 1.00 30.35 ? 155  ARG D C     1 
ATOM   8808  O  O     . ARG L  3 155 ? 83.258  93.599  133.410 1.00 31.68 ? 155  ARG D O     1 
ATOM   8809  C  CB    . ARG L  3 155 ? 83.172  90.283  133.426 1.00 31.22 ? 155  ARG D CB    1 
ATOM   8810  C  CG    . ARG L  3 155 ? 84.397  90.656  132.622 1.00 37.69 ? 155  ARG D CG    1 
ATOM   8811  C  CD    . ARG L  3 155 ? 85.577  89.764  132.969 1.00 44.37 ? 155  ARG D CD    1 
ATOM   8812  N  NE    . ARG L  3 155 ? 85.396  88.373  132.548 1.00 48.24 ? 155  ARG D NE    1 
ATOM   8813  C  CZ    . ARG L  3 155 ? 85.208  87.984  131.286 1.00 50.71 ? 155  ARG D CZ    1 
ATOM   8814  N  NH1   . ARG L  3 155 ? 85.166  88.881  130.305 1.00 51.22 ? 155  ARG D NH1   1 
ATOM   8815  N  NH2   . ARG L  3 155 ? 85.091  86.691  130.999 1.00 46.17 ? 155  ARG D NH2   1 
ATOM   8816  N  N     . ASN L  3 156 ? 81.419  92.701  132.481 1.00 28.64 ? 156  ASN D N     1 
ATOM   8817  C  CA    . ASN L  3 156 ? 81.224  93.803  131.538 1.00 30.51 ? 156  ASN D CA    1 
ATOM   8818  C  C     . ASN L  3 156 ? 80.100  94.786  131.861 1.00 32.32 ? 156  ASN D C     1 
ATOM   8819  O  O     . ASN L  3 156 ? 80.117  95.941  131.420 1.00 34.56 ? 156  ASN D O     1 
ATOM   8820  C  CB    . ASN L  3 156 ? 80.998  93.231  130.132 1.00 32.94 ? 156  ASN D CB    1 
ATOM   8821  C  CG    . ASN L  3 156 ? 82.148  92.345  129.678 1.00 36.00 ? 156  ASN D CG    1 
ATOM   8822  O  OD1   . ASN L  3 156 ? 83.309  92.681  129.885 1.00 35.55 ? 156  ASN D OD1   1 
ATOM   8823  N  ND2   . ASN L  3 156 ? 81.829  91.214  129.056 1.00 34.83 ? 156  ASN D ND2   1 
ATOM   8824  N  N     . GLU L  3 157 ? 79.123  94.325  132.621 1.00 28.89 ? 157  GLU D N     1 
ATOM   8825  C  CA    . GLU L  3 157 ? 77.981  95.150  132.976 1.00 28.20 ? 157  GLU D CA    1 
ATOM   8826  C  C     . GLU L  3 157 ? 77.524  94.760  134.359 1.00 26.86 ? 157  GLU D C     1 
ATOM   8827  O  O     . GLU L  3 157 ? 77.887  93.703  134.871 1.00 27.55 ? 157  GLU D O     1 
ATOM   8828  C  CB    . GLU L  3 157 ? 76.828  94.924  131.986 1.00 31.14 ? 157  GLU D CB    1 
ATOM   8829  C  CG    . GLU L  3 157 ? 77.192  95.114  130.527 1.00 32.01 ? 157  GLU D CG    1 
ATOM   8830  C  CD    . GLU L  3 157 ? 76.045  94.756  129.597 1.00 38.53 ? 157  GLU D CD    1 
ATOM   8831  O  OE1   . GLU L  3 157 ? 75.185  95.623  129.331 1.00 37.98 ? 157  GLU D OE1   1 
ATOM   8832  O  OE2   . GLU L  3 157 ? 75.987  93.592  129.140 1.00 35.99 ? 157  GLU D OE2   1 
ATOM   8833  N  N     . PHE L  3 158 ? 76.721  95.617  134.976 1.00 25.47 ? 158  PHE D N     1 
ATOM   8834  C  CA    . PHE L  3 158 ? 76.214  95.335  136.309 1.00 23.69 ? 158  PHE D CA    1 
ATOM   8835  C  C     . PHE L  3 158 ? 74.927  94.545  136.109 1.00 25.98 ? 158  PHE D C     1 
ATOM   8836  O  O     . PHE L  3 158 ? 73.837  95.111  136.021 1.00 27.18 ? 158  PHE D O     1 
ATOM   8837  C  CB    . PHE L  3 158 ? 75.940  96.650  137.046 1.00 26.62 ? 158  PHE D CB    1 
ATOM   8838  C  CG    . PHE L  3 158 ? 75.459  96.473  138.454 1.00 30.00 ? 158  PHE D CG    1 
ATOM   8839  C  CD1   . PHE L  3 158 ? 75.994  95.483  139.264 1.00 30.77 ? 158  PHE D CD1   1 
ATOM   8840  C  CD2   . PHE L  3 158 ? 74.484  97.317  138.982 1.00 29.89 ? 158  PHE D CD2   1 
ATOM   8841  C  CE1   . PHE L  3 158 ? 75.571  95.333  140.585 1.00 34.62 ? 158  PHE D CE1   1 
ATOM   8842  C  CE2   . PHE L  3 158 ? 74.059  97.174  140.294 1.00 32.04 ? 158  PHE D CE2   1 
ATOM   8843  C  CZ    . PHE L  3 158 ? 74.601  96.180  141.099 1.00 34.04 ? 158  PHE D CZ    1 
ATOM   8844  N  N     . LEU L  3 159 ? 75.064  93.224  136.035 1.00 24.21 ? 159  LEU D N     1 
ATOM   8845  C  CA    . LEU L  3 159 ? 73.918  92.348  135.801 1.00 22.83 ? 159  LEU D CA    1 
ATOM   8846  C  C     . LEU L  3 159 ? 73.164  91.859  137.033 1.00 22.24 ? 159  LEU D C     1 
ATOM   8847  O  O     . LEU L  3 159 ? 71.928  91.775  137.019 1.00 23.39 ? 159  LEU D O     1 
ATOM   8848  C  CB    . LEU L  3 159 ? 74.376  91.117  135.006 1.00 21.35 ? 159  LEU D CB    1 
ATOM   8849  C  CG    . LEU L  3 159 ? 75.048  91.370  133.663 1.00 21.62 ? 159  LEU D CG    1 
ATOM   8850  C  CD1   . LEU L  3 159 ? 75.371  90.011  133.020 1.00 22.47 ? 159  LEU D CD1   1 
ATOM   8851  C  CD2   . LEU L  3 159 ? 74.129  92.163  132.770 1.00 20.49 ? 159  LEU D CD2   1 
ATOM   8852  N  N     . VAL L  3 160 ? 73.891  91.488  138.084 1.00 22.89 ? 160  VAL D N     1 
ATOM   8853  C  CA    . VAL L  3 160 ? 73.242  90.965  139.278 1.00 25.31 ? 160  VAL D CA    1 
ATOM   8854  C  C     . VAL L  3 160 ? 73.787  91.515  140.589 1.00 26.72 ? 160  VAL D C     1 
ATOM   8855  O  O     . VAL L  3 160 ? 74.911  92.015  140.649 1.00 27.40 ? 160  VAL D O     1 
ATOM   8856  C  CB    . VAL L  3 160 ? 73.386  89.415  139.367 1.00 27.12 ? 160  VAL D CB    1 
ATOM   8857  C  CG1   . VAL L  3 160 ? 72.714  88.737  138.171 1.00 25.17 ? 160  VAL D CG1   1 
ATOM   8858  C  CG2   . VAL L  3 160 ? 74.866  89.035  139.428 1.00 26.34 ? 160  VAL D CG2   1 
ATOM   8859  N  N     . ASP L  3 161 ? 72.957  91.433  141.624 1.00 29.54 ? 161  ASP D N     1 
ATOM   8860  C  CA    . ASP L  3 161 ? 73.342  91.800  142.982 1.00 31.19 ? 161  ASP D CA    1 
ATOM   8861  C  C     . ASP L  3 161 ? 72.702  90.712  143.868 1.00 30.16 ? 161  ASP D C     1 
ATOM   8862  O  O     . ASP L  3 161 ? 72.217  89.713  143.343 1.00 29.67 ? 161  ASP D O     1 
ATOM   8863  C  CB    . ASP L  3 161 ? 72.915  93.241  143.346 1.00 34.36 ? 161  ASP D CB    1 
ATOM   8864  C  CG    . ASP L  3 161 ? 71.417  93.421  143.541 1.00 38.81 ? 161  ASP D CG    1 
ATOM   8865  O  OD1   . ASP L  3 161 ? 70.624  92.473  143.362 1.00 40.82 ? 161  ASP D OD1   1 
ATOM   8866  O  OD2   . ASP L  3 161 ? 71.032  94.563  143.888 1.00 40.77 ? 161  ASP D OD2   1 
ATOM   8867  N  N     . GLU L  3 162 ? 72.703  90.862  145.189 1.00 30.85 ? 162  GLU D N     1 
ATOM   8868  C  CA    . GLU L  3 162 ? 72.147  89.812  146.037 1.00 30.18 ? 162  GLU D CA    1 
ATOM   8869  C  C     . GLU L  3 162 ? 70.636  89.668  146.054 1.00 28.35 ? 162  GLU D C     1 
ATOM   8870  O  O     . GLU L  3 162 ? 70.126  88.749  146.674 1.00 32.21 ? 162  GLU D O     1 
ATOM   8871  C  CB    . GLU L  3 162 ? 72.634  89.968  147.480 1.00 34.92 ? 162  GLU D CB    1 
ATOM   8872  C  CG    . GLU L  3 162 ? 72.520  91.380  148.023 1.00 40.23 ? 162  GLU D CG    1 
ATOM   8873  C  CD    . GLU L  3 162 ? 73.455  92.335  147.298 1.00 45.17 ? 162  GLU D CD    1 
ATOM   8874  O  OE1   . GLU L  3 162 ? 74.636  91.964  147.103 1.00 49.84 ? 162  GLU D OE1   1 
ATOM   8875  O  OE2   . GLU L  3 162 ? 73.018  93.446  146.921 1.00 48.64 ? 162  GLU D OE2   1 
ATOM   8876  N  N     . ASN L  3 163 ? 69.914  90.539  145.360 1.00 27.24 ? 163  ASN D N     1 
ATOM   8877  C  CA    . ASN L  3 163 ? 68.459  90.464  145.375 1.00 29.15 ? 163  ASN D CA    1 
ATOM   8878  C  C     . ASN L  3 163 ? 67.790  90.069  144.066 1.00 28.67 ? 163  ASN D C     1 
ATOM   8879  O  O     . ASN L  3 163 ? 66.572  90.213  143.912 1.00 27.47 ? 163  ASN D O     1 
ATOM   8880  C  CB    . ASN L  3 163 ? 67.893  91.802  145.857 1.00 30.97 ? 163  ASN D CB    1 
ATOM   8881  C  CG    . ASN L  3 163 ? 68.468  92.210  147.200 1.00 31.34 ? 163  ASN D CG    1 
ATOM   8882  O  OD1   . ASN L  3 163 ? 68.359  91.471  148.173 1.00 32.84 ? 163  ASN D OD1   1 
ATOM   8883  N  ND2   . ASN L  3 163 ? 69.105  93.374  147.249 1.00 36.81 ? 163  ASN D ND2   1 
ATOM   8884  N  N     . ILE L  3 164 ? 68.573  89.563  143.123 1.00 24.90 ? 164  ILE D N     1 
ATOM   8885  C  CA    . ILE L  3 164 ? 68.017  89.155  141.831 1.00 23.34 ? 164  ILE D CA    1 
ATOM   8886  C  C     . ILE L  3 164 ? 68.754  87.870  141.428 1.00 23.26 ? 164  ILE D C     1 
ATOM   8887  O  O     . ILE L  3 164 ? 69.906  87.693  141.816 1.00 24.10 ? 164  ILE D O     1 
ATOM   8888  C  CB    . ILE L  3 164 ? 68.220  90.295  140.789 1.00 21.53 ? 164  ILE D CB    1 
ATOM   8889  C  CG1   . ILE L  3 164 ? 67.498  89.996  139.470 1.00 21.65 ? 164  ILE D CG1   1 
ATOM   8890  C  CG2   . ILE L  3 164 ? 69.689  90.533  140.561 1.00 22.37 ? 164  ILE D CG2   1 
ATOM   8891  C  CD1   . ILE L  3 164 ? 65.977  89.984  139.565 1.00 20.56 ? 164  ILE D CD1   1 
ATOM   8892  N  N     . ALA L  3 165 ? 68.081  86.982  140.681 1.00 23.32 ? 165  ALA D N     1 
ATOM   8893  C  CA    . ALA L  3 165 ? 68.671  85.707  140.242 1.00 23.36 ? 165  ALA D CA    1 
ATOM   8894  C  C     . ALA L  3 165 ? 69.359  85.040  141.428 1.00 23.85 ? 165  ALA D C     1 
ATOM   8895  O  O     . ALA L  3 165 ? 70.510  84.576  141.332 1.00 23.80 ? 165  ALA D O     1 
ATOM   8896  C  CB    . ALA L  3 165 ? 69.681  85.953  139.117 1.00 23.32 ? 165  ALA D CB    1 
ATOM   8897  N  N     . THR L  3 166 ? 68.642  84.973  142.546 1.00 22.26 ? 166  THR D N     1 
ATOM   8898  C  CA    . THR L  3 166 ? 69.197  84.423  143.768 1.00 23.89 ? 166  THR D CA    1 
ATOM   8899  C  C     . THR L  3 166 ? 69.308  82.908  143.840 1.00 22.14 ? 166  THR D C     1 
ATOM   8900  O  O     . THR L  3 166 ? 69.982  82.382  144.738 1.00 22.73 ? 166  THR D O     1 
ATOM   8901  C  CB    . THR L  3 166 ? 68.399  84.936  144.990 1.00 23.80 ? 166  THR D CB    1 
ATOM   8902  O  OG1   . THR L  3 166 ? 67.118  84.295  145.026 1.00 23.91 ? 166  THR D OG1   1 
ATOM   8903  C  CG2   . THR L  3 166 ? 68.193  86.445  144.876 1.00 23.77 ? 166  THR D CG2   1 
ATOM   8904  N  N     . TYR L  3 167 ? 68.679  82.198  142.893 1.00 19.71 ? 167  TYR D N     1 
ATOM   8905  C  CA    . TYR L  3 167 ? 68.725  80.737  142.865 1.00 18.59 ? 167  TYR D CA    1 
ATOM   8906  C  C     . TYR L  3 167 ? 69.487  80.184  141.641 1.00 16.81 ? 167  TYR D C     1 
ATOM   8907  O  O     . TYR L  3 167 ? 69.568  78.973  141.454 1.00 20.06 ? 167  TYR D O     1 
ATOM   8908  C  CB    . TYR L  3 167 ? 67.316  80.147  142.860 1.00 20.80 ? 167  TYR D CB    1 
ATOM   8909  C  CG    . TYR L  3 167 ? 66.521  80.586  144.053 1.00 21.45 ? 167  TYR D CG    1 
ATOM   8910  C  CD1   . TYR L  3 167 ? 65.409  81.405  143.905 1.00 21.80 ? 167  TYR D CD1   1 
ATOM   8911  C  CD2   . TYR L  3 167 ? 66.915  80.212  145.336 1.00 25.27 ? 167  TYR D CD2   1 
ATOM   8912  C  CE1   . TYR L  3 167 ? 64.690  81.851  145.031 1.00 26.97 ? 167  TYR D CE1   1 
ATOM   8913  C  CE2   . TYR L  3 167 ? 66.215  80.646  146.471 1.00 26.96 ? 167  TYR D CE2   1 
ATOM   8914  C  CZ    . TYR L  3 167 ? 65.109  81.464  146.305 1.00 26.03 ? 167  TYR D CZ    1 
ATOM   8915  O  OH    . TYR L  3 167 ? 64.417  81.907  147.413 1.00 29.79 ? 167  TYR D OH    1 
ATOM   8916  N  N     . ALA L  3 168 ? 70.046  81.077  140.827 1.00 20.84 ? 168  ALA D N     1 
ATOM   8917  C  CA    . ALA L  3 168 ? 70.785  80.639  139.629 1.00 19.53 ? 168  ALA D CA    1 
ATOM   8918  C  C     . ALA L  3 168 ? 71.898  79.660  140.023 1.00 22.69 ? 168  ALA D C     1 
ATOM   8919  O  O     . ALA L  3 168 ? 72.719  79.951  140.901 1.00 20.22 ? 168  ALA D O     1 
ATOM   8920  C  CB    . ALA L  3 168 ? 71.362  81.839  138.916 1.00 19.18 ? 168  ALA D CB    1 
ATOM   8921  N  N     . SER L  3 169 ? 71.914  78.498  139.380 1.00 18.53 ? 169  SER D N     1 
ATOM   8922  C  CA    . SER L  3 169 ? 72.894  77.450  139.681 1.00 22.24 ? 169  SER D CA    1 
ATOM   8923  C  C     . SER L  3 169 ? 74.371  77.850  139.626 1.00 22.61 ? 169  SER D C     1 
ATOM   8924  O  O     . SER L  3 169 ? 75.176  77.360  140.418 1.00 22.91 ? 169  SER D O     1 
ATOM   8925  C  CB    . SER L  3 169 ? 72.681  76.265  138.736 1.00 23.80 ? 169  SER D CB    1 
ATOM   8926  O  OG    . SER L  3 169 ? 71.341  75.795  138.775 1.00 25.52 ? 169  SER D OG    1 
ATOM   8927  N  N     . LEU L  3 170 ? 74.726  78.725  138.702 1.00 19.21 ? 170  LEU D N     1 
ATOM   8928  C  CA    . LEU L  3 170 ? 76.119  79.136  138.553 1.00 22.08 ? 170  LEU D CA    1 
ATOM   8929  C  C     . LEU L  3 170 ? 76.691  79.996  139.665 1.00 24.70 ? 170  LEU D C     1 
ATOM   8930  O  O     . LEU L  3 170 ? 77.901  80.029  139.842 1.00 25.78 ? 170  LEU D O     1 
ATOM   8931  C  CB    . LEU L  3 170 ? 76.327  79.865  137.230 1.00 20.74 ? 170  LEU D CB    1 
ATOM   8932  C  CG    . LEU L  3 170 ? 76.342  78.919  136.028 1.00 18.33 ? 170  LEU D CG    1 
ATOM   8933  C  CD1   . LEU L  3 170 ? 76.160  79.770  134.781 1.00 16.66 ? 170  LEU D CD1   1 
ATOM   8934  C  CD2   . LEU L  3 170 ? 77.633  78.078  135.992 1.00 19.75 ? 170  LEU D CD2   1 
ATOM   8935  N  N     . ARG L  3 171 ? 75.831  80.661  140.426 1.00 25.13 ? 171  ARG D N     1 
ATOM   8936  C  CA    . ARG L  3 171 ? 76.307  81.552  141.471 1.00 26.63 ? 171  ARG D CA    1 
ATOM   8937  C  C     . ARG L  3 171 ? 76.859  80.873  142.700 1.00 28.34 ? 171  ARG D C     1 
ATOM   8938  O  O     . ARG L  3 171 ? 76.212  80.030  143.302 1.00 29.15 ? 171  ARG D O     1 
ATOM   8939  C  CB    . ARG L  3 171 ? 75.196  82.523  141.851 1.00 26.69 ? 171  ARG D CB    1 
ATOM   8940  C  CG    . ARG L  3 171 ? 74.713  83.303  140.626 1.00 28.15 ? 171  ARG D CG    1 
ATOM   8941  C  CD    . ARG L  3 171 ? 73.757  84.392  141.001 1.00 31.80 ? 171  ARG D CD    1 
ATOM   8942  N  NE    . ARG L  3 171 ? 74.429  85.479  141.719 1.00 29.22 ? 171  ARG D NE    1 
ATOM   8943  C  CZ    . ARG L  3 171 ? 73.795  86.564  142.158 1.00 31.33 ? 171  ARG D CZ    1 
ATOM   8944  N  NH1   . ARG L  3 171 ? 72.491  86.695  141.950 1.00 27.67 ? 171  ARG D NH1   1 
ATOM   8945  N  NH2   . ARG L  3 171 ? 74.454  87.511  142.807 1.00 30.91 ? 171  ARG D NH2   1 
ATOM   8946  N  N     . ALA L  3 172 ? 78.086  81.250  143.053 1.00 33.07 ? 172  ALA D N     1 
ATOM   8947  C  CA    . ALA L  3 172 ? 78.752  80.692  144.224 1.00 39.26 ? 172  ALA D CA    1 
ATOM   8948  C  C     . ALA L  3 172 ? 78.210  81.386  145.474 1.00 42.90 ? 172  ALA D C     1 
ATOM   8949  O  O     . ALA L  3 172 ? 77.810  82.548  145.401 1.00 45.98 ? 172  ALA D O     1 
ATOM   8950  C  CB    . ALA L  3 172 ? 80.251  80.924  144.108 1.00 40.32 ? 172  ALA D CB    1 
ATOM   8951  N  N     . GLY L  3 173 ? 78.157  80.693  146.612 1.00 47.87 ? 173  GLY D N     1 
ATOM   8952  C  CA    . GLY L  3 173 ? 77.681  81.389  147.801 1.00 53.52 ? 173  GLY D CA    1 
ATOM   8953  C  C     . GLY L  3 173 ? 76.793  80.786  148.877 1.00 56.24 ? 173  GLY D C     1 
ATOM   8954  O  O     . GLY L  3 173 ? 76.997  81.073  150.064 1.00 56.61 ? 173  GLY D O     1 
ATOM   8955  N  N     . ASN L  3 174 ? 75.800  79.986  148.503 1.00 58.72 ? 174  ASN D N     1 
ATOM   8956  C  CA    . ASN L  3 174 ? 74.909  79.402  149.508 1.00 59.31 ? 174  ASN D CA    1 
ATOM   8957  C  C     . ASN L  3 174 ? 75.067  77.894  149.641 1.00 59.36 ? 174  ASN D C     1 
ATOM   8958  O  O     . ASN L  3 174 ? 74.096  77.146  149.495 1.00 60.03 ? 174  ASN D O     1 
ATOM   8959  C  CB    . ASN L  3 174 ? 73.445  79.728  149.184 1.00 60.04 ? 174  ASN D CB    1 
ATOM   8960  C  CG    . ASN L  3 174 ? 73.082  81.173  149.490 1.00 60.04 ? 174  ASN D CG    1 
ATOM   8961  O  OD1   . ASN L  3 174 ? 73.224  81.635  150.627 1.00 60.04 ? 174  ASN D OD1   1 
ATOM   8962  N  ND2   . ASN L  3 174 ? 72.600  81.892  148.477 1.00 60.04 ? 174  ASN D ND2   1 
ATOM   8963  N  N     . GLY L  3 175 ? 76.289  77.452  149.924 1.00 59.87 ? 175  GLY D N     1 
ATOM   8964  C  CA    . GLY L  3 175 ? 76.547  76.028  150.062 1.00 59.14 ? 175  GLY D CA    1 
ATOM   8965  C  C     . GLY L  3 175 ? 76.350  75.256  148.765 1.00 57.87 ? 175  GLY D C     1 
ATOM   8966  O  O     . GLY L  3 175 ? 76.610  74.052  148.711 1.00 59.04 ? 175  GLY D O     1 
ATOM   8967  N  N     . ASN L  3 176 ? 75.888  75.945  147.723 1.00 54.32 ? 176  ASN D N     1 
ATOM   8968  C  CA    . ASN L  3 176 ? 75.659  75.326  146.420 1.00 51.87 ? 176  ASN D CA    1 
ATOM   8969  C  C     . ASN L  3 176 ? 76.948  74.697  145.904 1.00 46.32 ? 176  ASN D C     1 
ATOM   8970  O  O     . ASN L  3 176 ? 78.013  75.299  145.966 1.00 46.30 ? 176  ASN D O     1 
ATOM   8971  C  CB    . ASN L  3 176 ? 75.144  76.368  145.429 1.00 54.18 ? 176  ASN D CB    1 
ATOM   8972  C  CG    . ASN L  3 176 ? 73.786  76.920  145.825 1.00 58.58 ? 176  ASN D CG    1 
ATOM   8973  O  OD1   . ASN L  3 176 ? 72.788  76.190  145.855 1.00 60.03 ? 176  ASN D OD1   1 
ATOM   8974  N  ND2   . ASN L  3 176 ? 73.740  78.212  146.140 1.00 60.04 ? 176  ASN D ND2   1 
ATOM   8975  N  N     . MET L  3 177 ? 76.832  73.488  145.374 1.00 43.22 ? 177  MET D N     1 
ATOM   8976  C  CA    . MET L  3 177 ? 77.984  72.736  144.887 1.00 37.63 ? 177  MET D CA    1 
ATOM   8977  C  C     . MET L  3 177 ? 78.310  72.926  143.405 1.00 32.07 ? 177  MET D C     1 
ATOM   8978  O  O     . MET L  3 177 ? 77.556  73.565  142.663 1.00 30.49 ? 177  MET D O     1 
ATOM   8979  C  CB    . MET L  3 177 ? 77.737  71.258  145.164 1.00 39.51 ? 177  MET D CB    1 
ATOM   8980  C  CG    . MET L  3 177 ? 77.536  70.928  146.641 1.00 45.60 ? 177  MET D CG    1 
ATOM   8981  S  SD    . MET L  3 177 ? 76.335  69.595  146.889 1.00 50.53 ? 177  MET D SD    1 
ATOM   8982  C  CE    . MET L  3 177 ? 74.843  70.563  147.001 1.00 49.58 ? 177  MET D CE    1 
ATOM   8983  N  N     . PRO L  3 178 ? 79.456  72.381  142.953 1.00 28.35 ? 178  PRO D N     1 
ATOM   8984  C  CA    . PRO L  3 178 ? 79.750  72.560  141.528 1.00 25.47 ? 178  PRO D CA    1 
ATOM   8985  C  C     . PRO L  3 178 ? 78.773  71.741  140.694 1.00 20.56 ? 178  PRO D C     1 
ATOM   8986  O  O     . PRO L  3 178 ? 78.083  70.867  141.205 1.00 22.11 ? 178  PRO D O     1 
ATOM   8987  C  CB    . PRO L  3 178 ? 81.187  72.059  141.387 1.00 24.25 ? 178  PRO D CB    1 
ATOM   8988  C  CG    . PRO L  3 178 ? 81.320  71.072  142.499 1.00 32.92 ? 178  PRO D CG    1 
ATOM   8989  C  CD    . PRO L  3 178 ? 80.564  71.697  143.644 1.00 28.62 ? 178  PRO D CD    1 
ATOM   8990  N  N     . LEU L  3 179 ? 78.741  72.027  139.397 1.00 17.24 ? 179  LEU D N     1 
ATOM   8991  C  CA    . LEU L  3 179 ? 77.830  71.350  138.484 1.00 16.10 ? 179  LEU D CA    1 
ATOM   8992  C  C     . LEU L  3 179 ? 78.466  70.164  137.781 1.00 18.48 ? 179  LEU D C     1 
ATOM   8993  O  O     . LEU L  3 179 ? 79.652  70.208  137.442 1.00 17.81 ? 179  LEU D O     1 
ATOM   8994  C  CB    . LEU L  3 179 ? 77.362  72.362  137.434 1.00 16.84 ? 179  LEU D CB    1 
ATOM   8995  C  CG    . LEU L  3 179 ? 76.436  73.434  138.027 1.00 22.30 ? 179  LEU D CG    1 
ATOM   8996  C  CD1   . LEU L  3 179 ? 76.573  74.747  137.279 1.00 22.41 ? 179  LEU D CD1   1 
ATOM   8997  C  CD2   . LEU L  3 179 ? 75.002  72.911  137.955 1.00 24.22 ? 179  LEU D CD2   1 
ATOM   8998  N  N     . LEU L  3 180 ? 77.688  69.100  137.576 1.00 15.27 ? 180  LEU D N     1 
ATOM   8999  C  CA    . LEU L  3 180 ? 78.207  67.946  136.843 1.00 16.85 ? 180  LEU D CA    1 
ATOM   9000  C  C     . LEU L  3 180 ? 77.974  68.252  135.358 1.00 16.79 ? 180  LEU D C     1 
ATOM   9001  O  O     . LEU L  3 180 ? 76.834  68.415  134.924 1.00 19.55 ? 180  LEU D O     1 
ATOM   9002  C  CB    . LEU L  3 180 ? 77.477  66.664  137.244 1.00 16.70 ? 180  LEU D CB    1 
ATOM   9003  C  CG    . LEU L  3 180 ? 77.916  65.406  136.482 1.00 17.82 ? 180  LEU D CG    1 
ATOM   9004  C  CD1   . LEU L  3 180 ? 79.390  65.096  136.786 1.00 20.57 ? 180  LEU D CD1   1 
ATOM   9005  C  CD2   . LEU L  3 180 ? 77.028  64.240  136.857 1.00 18.82 ? 180  LEU D CD2   1 
ATOM   9006  N  N     . HIS L  3 181 ? 79.060  68.319  134.595 1.00 13.59 ? 181  HIS D N     1 
ATOM   9007  C  CA    . HIS L  3 181 ? 78.994  68.633  133.165 1.00 12.58 ? 181  HIS D CA    1 
ATOM   9008  C  C     . HIS L  3 181 ? 78.845  67.382  132.281 1.00 15.04 ? 181  HIS D C     1 
ATOM   9009  O  O     . HIS L  3 181 ? 78.065  67.374  131.310 1.00 14.53 ? 181  HIS D O     1 
ATOM   9010  C  CB    . HIS L  3 181 ? 80.268  69.403  132.768 1.00 14.13 ? 181  HIS D CB    1 
ATOM   9011  C  CG    . HIS L  3 181 ? 80.288  69.831  131.324 1.00 13.32 ? 181  HIS D CG    1 
ATOM   9012  N  ND1   . HIS L  3 181 ? 79.386  70.731  130.809 1.00 16.02 ? 181  HIS D ND1   1 
ATOM   9013  C  CD2   . HIS L  3 181 ? 81.102  69.471  130.300 1.00 13.86 ? 181  HIS D CD2   1 
ATOM   9014  C  CE1   . HIS L  3 181 ? 79.646  70.919  129.522 1.00 16.27 ? 181  HIS D CE1   1 
ATOM   9015  N  NE2   . HIS L  3 181 ? 80.683  70.170  129.192 1.00 14.27 ? 181  HIS D NE2   1 
ATOM   9016  N  N     . ALA L  3 182 ? 79.587  66.332  132.618 1.00 13.31 ? 182  ALA D N     1 
ATOM   9017  C  CA    . ALA L  3 182 ? 79.543  65.111  131.812 1.00 14.32 ? 182  ALA D CA    1 
ATOM   9018  C  C     . ALA L  3 182 ? 79.837  63.852  132.583 1.00 15.47 ? 182  ALA D C     1 
ATOM   9019  O  O     . ALA L  3 182 ? 80.608  63.860  133.533 1.00 14.91 ? 182  ALA D O     1 
ATOM   9020  C  CB    . ALA L  3 182 ? 80.573  65.208  130.653 1.00 14.78 ? 182  ALA D CB    1 
ATOM   9021  N  N     . SER L  3 183 ? 79.195  62.772  132.149 1.00 13.57 ? 183  SER D N     1 
ATOM   9022  C  CA    . SER L  3 183 ? 79.454  61.435  132.652 1.00 13.33 ? 183  SER D CA    1 
ATOM   9023  C  C     . SER L  3 183 ? 80.101  60.734  131.433 1.00 12.33 ? 183  SER D C     1 
ATOM   9024  O  O     . SER L  3 183 ? 79.490  60.660  130.355 1.00 13.51 ? 183  SER D O     1 
ATOM   9025  C  CB    . SER L  3 183 ? 78.140  60.720  132.995 1.00 14.59 ? 183  SER D CB    1 
ATOM   9026  O  OG    . SER L  3 183 ? 78.366  59.311  133.033 1.00 16.78 ? 183  SER D OG    1 
ATOM   9027  N  N     . ILE L  3 184 ? 81.327  60.238  131.595 1.00 11.25 ? 184  ILE D N     1 
ATOM   9028  C  CA    . ILE L  3 184 ? 82.016  59.560  130.492 1.00 15.18 ? 184  ILE D CA    1 
ATOM   9029  C  C     . ILE L  3 184 ? 82.286  58.134  130.915 1.00 15.56 ? 184  ILE D C     1 
ATOM   9030  O  O     . ILE L  3 184 ? 83.093  57.904  131.816 1.00 16.31 ? 184  ILE D O     1 
ATOM   9031  C  CB    . ILE L  3 184 ? 83.357  60.260  130.155 1.00 13.03 ? 184  ILE D CB    1 
ATOM   9032  C  CG1   . ILE L  3 184 ? 83.072  61.735  129.835 1.00 12.20 ? 184  ILE D CG1   1 
ATOM   9033  C  CG2   . ILE L  3 184 ? 84.094  59.519  128.986 1.00 15.42 ? 184  ILE D CG2   1 
ATOM   9034  C  CD1   . ILE L  3 184 ? 84.343  62.578  129.620 1.00 16.01 ? 184  ILE D CD1   1 
ATOM   9035  N  N     . SER L  3 185 ? 81.605  57.185  130.269 1.00 11.93 ? 185  SER D N     1 
ATOM   9036  C  CA    . SER L  3 185 ? 81.770  55.757  130.576 1.00 12.55 ? 185  SER D CA    1 
ATOM   9037  C  C     . SER L  3 185 ? 82.805  55.196  129.623 1.00 13.05 ? 185  SER D C     1 
ATOM   9038  O  O     . SER L  3 185 ? 82.788  55.520  128.431 1.00 16.93 ? 185  SER D O     1 
ATOM   9039  C  CB    . SER L  3 185 ? 80.473  54.988  130.339 1.00 15.85 ? 185  SER D CB    1 
ATOM   9040  O  OG    . SER L  3 185 ? 79.434  55.432  131.206 1.00 19.80 ? 185  SER D OG    1 
ATOM   9041  N  N     . CYS L  3 186 ? 83.699  54.362  130.141 1.00 10.92 ? 186  CYS D N     1 
ATOM   9042  C  CA    . CYS L  3 186 ? 84.729  53.764  129.293 1.00 11.49 ? 186  CYS D CA    1 
ATOM   9043  C  C     . CYS L  3 186 ? 84.592  52.262  129.261 1.00 12.68 ? 186  CYS D C     1 
ATOM   9044  O  O     . CYS L  3 186 ? 84.246  51.648  130.272 1.00 12.19 ? 186  CYS D O     1 
ATOM   9045  C  CB    . CYS L  3 186 ? 86.131  54.099  129.813 1.00 13.16 ? 186  CYS D CB    1 
ATOM   9046  S  SG    . CYS L  3 186 ? 86.491  55.877  129.875 1.00 15.08 ? 186  CYS D SG    1 
ATOM   9047  N  N     . LYS L  3 187 ? 84.812  51.670  128.087 1.00 13.74 ? 187  LYS D N     1 
ATOM   9048  C  CA    . LYS L  3 187 ? 84.790  50.208  127.963 1.00 13.44 ? 187  LYS D CA    1 
ATOM   9049  C  C     . LYS L  3 187 ? 85.942  49.830  127.037 1.00 13.35 ? 187  LYS D C     1 
ATOM   9050  O  O     . LYS L  3 187 ? 85.916  50.122  125.825 1.00 13.06 ? 187  LYS D O     1 
ATOM   9051  C  CB    . LYS L  3 187 ? 83.438  49.711  127.404 1.00 13.71 ? 187  LYS D CB    1 
ATOM   9052  C  CG    . LYS L  3 187 ? 82.299  50.046  128.379 1.00 13.76 ? 187  LYS D CG    1 
ATOM   9053  C  CD    . LYS L  3 187 ? 80.972  49.402  128.000 1.00 13.55 ? 187  LYS D CD    1 
ATOM   9054  C  CE    . LYS L  3 187 ? 79.922  49.630  129.118 1.00 15.60 ? 187  LYS D CE    1 
ATOM   9055  N  NZ    . LYS L  3 187 ? 80.341  49.007  130.429 1.00 18.32 ? 187  LYS D NZ    1 
ATOM   9056  N  N     . TRP L  3 188 ? 86.971  49.188  127.582 1.00 12.12 ? 188  TRP D N     1 
ATOM   9057  C  CA    . TRP L  3 188 ? 88.128  48.778  126.765 1.00 13.53 ? 188  TRP D CA    1 
ATOM   9058  C  C     . TRP L  3 188 ? 87.667  47.828  125.644 1.00 14.21 ? 188  TRP D C     1 
ATOM   9059  O  O     . TRP L  3 188 ? 88.059  47.984  124.481 1.00 13.86 ? 188  TRP D O     1 
ATOM   9060  C  CB    . TRP L  3 188 ? 89.192  48.116  127.660 1.00 13.73 ? 188  TRP D CB    1 
ATOM   9061  C  CG    . TRP L  3 188 ? 90.364  47.545  126.921 1.00 16.33 ? 188  TRP D CG    1 
ATOM   9062  C  CD1   . TRP L  3 188 ? 90.775  46.248  126.946 1.00 14.12 ? 188  TRP D CD1   1 
ATOM   9063  C  CD2   . TRP L  3 188 ? 91.272  48.239  126.048 1.00 16.04 ? 188  TRP D CD2   1 
ATOM   9064  N  NE1   . TRP L  3 188 ? 91.880  46.082  126.141 1.00 13.74 ? 188  TRP D NE1   1 
ATOM   9065  C  CE2   . TRP L  3 188 ? 92.203  47.288  125.576 1.00 14.53 ? 188  TRP D CE2   1 
ATOM   9066  C  CE3   . TRP L  3 188 ? 91.384  49.569  125.618 1.00 15.22 ? 188  TRP D CE3   1 
ATOM   9067  C  CZ2   . TRP L  3 188 ? 93.244  47.626  124.691 1.00 15.03 ? 188  TRP D CZ2   1 
ATOM   9068  C  CZ3   . TRP L  3 188 ? 92.418  49.904  124.740 1.00 17.92 ? 188  TRP D CZ3   1 
ATOM   9069  C  CH2   . TRP L  3 188 ? 93.329  48.931  124.287 1.00 14.27 ? 188  TRP D CH2   1 
ATOM   9070  N  N     . THR L  3 189 ? 86.856  46.840  126.007 1.00 11.94 ? 189  THR D N     1 
ATOM   9071  C  CA    . THR L  3 189 ? 86.249  45.928  125.052 1.00 12.14 ? 189  THR D CA    1 
ATOM   9072  C  C     . THR L  3 189 ? 84.806  45.774  125.525 1.00 14.37 ? 189  THR D C     1 
ATOM   9073  O  O     . THR L  3 189 ? 84.435  46.179  126.642 1.00 13.01 ? 189  THR D O     1 
ATOM   9074  C  CB    . THR L  3 189 ? 86.890  44.551  125.034 1.00 15.57 ? 189  THR D CB    1 
ATOM   9075  O  OG1   . THR L  3 189 ? 86.728  43.927  126.322 1.00 14.44 ? 189  THR D OG1   1 
ATOM   9076  C  CG2   . THR L  3 189 ? 88.377  44.662  124.680 1.00 13.54 ? 189  THR D CG2   1 
ATOM   9077  N  N     . ILE L  3 190 ? 83.993  45.178  124.674 1.00 11.40 ? 190  ILE D N     1 
ATOM   9078  C  CA    . ILE L  3 190 ? 82.593  44.991  124.953 1.00 11.36 ? 190  ILE D CA    1 
ATOM   9079  C  C     . ILE L  3 190 ? 82.108  43.557  124.765 1.00 14.92 ? 190  ILE D C     1 
ATOM   9080  O  O     . ILE L  3 190 ? 82.644  42.818  123.939 1.00 13.38 ? 190  ILE D O     1 
ATOM   9081  C  CB    . ILE L  3 190 ? 81.746  45.902  123.964 1.00 11.59 ? 190  ILE D CB    1 
ATOM   9082  C  CG1   . ILE L  3 190 ? 81.895  47.383  124.346 1.00 11.87 ? 190  ILE D CG1   1 
ATOM   9083  C  CG2   . ILE L  3 190 ? 80.266  45.477  123.955 1.00 12.73 ? 190  ILE D CG2   1 
ATOM   9084  C  CD1   . ILE L  3 190 ? 81.358  48.370  123.264 1.00 14.23 ? 190  ILE D CD1   1 
ATOM   9085  N  N     . ARG L  3 191 ? 81.147  43.160  125.605 1.00 14.28 ? 191  ARG D N     1 
ATOM   9086  C  CA    . ARG L  3 191 ? 80.356  41.943  125.381 1.00 11.86 ? 191  ARG D CA    1 
ATOM   9087  C  C     . ARG L  3 191 ? 78.945  42.545  125.527 1.00 12.62 ? 191  ARG D C     1 
ATOM   9088  O  O     . ARG L  3 191 ? 78.716  43.443  126.380 1.00 13.33 ? 191  ARG D O     1 
ATOM   9089  C  CB    . ARG L  3 191 ? 80.592  40.830  126.410 1.00 13.12 ? 191  ARG D CB    1 
ATOM   9090  C  CG    . ARG L  3 191 ? 81.975  40.194  126.293 1.00 12.30 ? 191  ARG D CG    1 
ATOM   9091  C  CD    . ARG L  3 191 ? 82.220  39.491  124.925 1.00 13.09 ? 191  ARG D CD    1 
ATOM   9092  N  NE    . ARG L  3 191 ? 83.521  38.828  124.982 1.00 13.03 ? 191  ARG D NE    1 
ATOM   9093  C  CZ    . ARG L  3 191 ? 84.684  39.380  124.653 1.00 14.61 ? 191  ARG D CZ    1 
ATOM   9094  N  NH1   . ARG L  3 191 ? 84.762  40.636  124.192 1.00 14.12 ? 191  ARG D NH1   1 
ATOM   9095  N  NH2   . ARG L  3 191 ? 85.803  38.692  124.852 1.00 17.27 ? 191  ARG D NH2   1 
ATOM   9096  N  N     . SER L  3 192 ? 78.002  42.074  124.719 1.00 12.64 ? 192  SER D N     1 
ATOM   9097  C  CA    . SER L  3 192 ? 76.675  42.682  124.712 1.00 12.53 ? 192  SER D CA    1 
ATOM   9098  C  C     . SER L  3 192 ? 75.911  42.653  126.019 1.00 13.43 ? 192  SER D C     1 
ATOM   9099  O  O     . SER L  3 192 ? 75.028  43.491  126.222 1.00 15.89 ? 192  SER D O     1 
ATOM   9100  C  CB    . SER L  3 192 ? 75.823  42.098  123.585 1.00 17.01 ? 192  SER D CB    1 
ATOM   9101  O  OG    . SER L  3 192 ? 75.653  40.711  123.775 1.00 18.19 ? 192  SER D OG    1 
ATOM   9102  N  N     . ASP L  3 193 ? 76.241  41.718  126.915 1.00 15.55 ? 193  ASP D N     1 
ATOM   9103  C  CA    . ASP L  3 193 ? 75.572  41.689  128.209 1.00 15.52 ? 193  ASP D CA    1 
ATOM   9104  C  C     . ASP L  3 193 ? 76.113  42.753  129.143 1.00 17.22 ? 193  ASP D C     1 
ATOM   9105  O  O     . ASP L  3 193 ? 75.346  43.563  129.710 1.00 18.35 ? 193  ASP D O     1 
ATOM   9106  C  CB    . ASP L  3 193 ? 75.685  40.296  128.898 1.00 14.75 ? 193  ASP D CB    1 
ATOM   9107  C  CG    . ASP L  3 193 ? 77.123  39.811  129.083 1.00 17.48 ? 193  ASP D CG    1 
ATOM   9108  O  OD1   . ASP L  3 193 ? 77.392  39.133  130.105 1.00 15.52 ? 193  ASP D OD1   1 
ATOM   9109  O  OD2   . ASP L  3 193 ? 77.987  40.066  128.213 1.00 17.02 ? 193  ASP D OD2   1 
ATOM   9110  N  N     . ARG L  3 194 ? 77.434  42.778  129.315 1.00 14.89 ? 194  ARG D N     1 
ATOM   9111  C  CA    . ARG L  3 194 ? 78.027  43.732  130.243 1.00 16.65 ? 194  ARG D CA    1 
ATOM   9112  C  C     . ARG L  3 194 ? 78.056  45.158  129.745 1.00 18.08 ? 194  ARG D C     1 
ATOM   9113  O  O     . ARG L  3 194 ? 78.328  46.082  130.517 1.00 23.79 ? 194  ARG D O     1 
ATOM   9114  C  CB    . ARG L  3 194 ? 79.433  43.270  130.678 1.00 16.03 ? 194  ARG D CB    1 
ATOM   9115  C  CG    . ARG L  3 194 ? 80.473  43.021  129.569 1.00 16.89 ? 194  ARG D CG    1 
ATOM   9116  C  CD    . ARG L  3 194 ? 81.813  42.558  130.196 1.00 16.42 ? 194  ARG D CD    1 
ATOM   9117  N  NE    . ARG L  3 194 ? 82.796  42.101  129.199 1.00 14.85 ? 194  ARG D NE    1 
ATOM   9118  C  CZ    . ARG L  3 194 ? 83.508  42.918  128.436 1.00 16.50 ? 194  ARG D CZ    1 
ATOM   9119  N  NH1   . ARG L  3 194 ? 83.356  44.238  128.561 1.00 14.94 ? 194  ARG D NH1   1 
ATOM   9120  N  NH2   . ARG L  3 194 ? 84.349  42.410  127.531 1.00 15.63 ? 194  ARG D NH2   1 
ATOM   9121  N  N     . ALA L  3 195 ? 77.770  45.366  128.463 1.00 15.05 ? 195  ALA D N     1 
ATOM   9122  C  CA    . ALA L  3 195 ? 77.743  46.731  127.945 1.00 17.75 ? 195  ALA D CA    1 
ATOM   9123  C  C     . ALA L  3 195 ? 76.503  47.495  128.429 1.00 13.96 ? 195  ALA D C     1 
ATOM   9124  O  O     . ALA L  3 195 ? 76.486  48.731  128.418 1.00 15.26 ? 195  ALA D O     1 
ATOM   9125  C  CB    . ALA L  3 195 ? 77.735  46.721  126.433 1.00 21.23 ? 195  ALA D CB    1 
ATOM   9126  N  N     . GLN L  3 196 ? 75.474  46.758  128.858 1.00 13.53 ? 196  GLN D N     1 
ATOM   9127  C  CA    . GLN L  3 196 ? 74.227  47.404  129.244 1.00 11.95 ? 196  GLN D CA    1 
ATOM   9128  C  C     . GLN L  3 196 ? 74.243  48.239  130.518 1.00 12.25 ? 196  GLN D C     1 
ATOM   9129  O  O     . GLN L  3 196 ? 73.305  49.003  130.749 1.00 12.50 ? 196  GLN D O     1 
ATOM   9130  C  CB    . GLN L  3 196 ? 73.102  46.370  129.290 1.00 12.71 ? 196  GLN D CB    1 
ATOM   9131  C  CG    . GLN L  3 196 ? 72.993  45.559  127.996 1.00 12.45 ? 196  GLN D CG    1 
ATOM   9132  C  CD    . GLN L  3 196 ? 72.906  46.423  126.745 1.00 15.50 ? 196  GLN D CD    1 
ATOM   9133  O  OE1   . GLN L  3 196 ? 72.236  47.445  126.731 1.00 18.44 ? 196  GLN D OE1   1 
ATOM   9134  N  NE2   . GLN L  3 196 ? 73.592  45.998  125.673 1.00 13.28 ? 196  GLN D NE2   1 
ATOM   9135  N  N     . ASN L  3 197 ? 75.284  48.119  131.339 1.00 13.32 ? 197  ASN D N     1 
ATOM   9136  C  CA    . ASN L  3 197 ? 75.310  48.979  132.529 1.00 11.77 ? 197  ASN D CA    1 
ATOM   9137  C  C     . ASN L  3 197 ? 75.462  50.461  132.141 1.00 14.09 ? 197  ASN D C     1 
ATOM   9138  O  O     . ASN L  3 197 ? 75.136  51.336  132.919 1.00 15.00 ? 197  ASN D O     1 
ATOM   9139  C  CB    . ASN L  3 197 ? 76.373  48.513  133.578 1.00 14.84 ? 197  ASN D CB    1 
ATOM   9140  C  CG    . ASN L  3 197 ? 77.830  48.640  133.113 1.00 15.38 ? 197  ASN D CG    1 
ATOM   9141  O  OD1   . ASN L  3 197 ? 78.044  48.825  131.815 1.00 20.14 ? 197  ASN D OD1   1 
ATOM   9142  N  ND2   . ASN L  3 197 ? 78.763  48.550  133.936 1.00 10.81 ? 197  ASN D ND2   1 
ATOM   9143  N  N     . ALA L  3 198 ? 75.902  50.746  130.907 1.00 13.68 ? 198  ALA D N     1 
ATOM   9144  C  CA    . ALA L  3 198 ? 75.996  52.142  130.485 1.00 14.39 ? 198  ALA D CA    1 
ATOM   9145  C  C     . ALA L  3 198 ? 74.573  52.711  130.323 1.00 13.62 ? 198  ALA D C     1 
ATOM   9146  O  O     . ALA L  3 198 ? 74.346  53.904  130.552 1.00 15.46 ? 198  ALA D O     1 
ATOM   9147  C  CB    . ALA L  3 198 ? 76.768  52.260  129.141 1.00 16.32 ? 198  ALA D CB    1 
ATOM   9148  N  N     . ARG L  3 199 ? 73.638  51.869  129.892 1.00 14.40 ? 199  ARG D N     1 
ATOM   9149  C  CA    . ARG L  3 199 ? 72.252  52.300  129.725 1.00 14.69 ? 199  ARG D CA    1 
ATOM   9150  C  C     . ARG L  3 199 ? 71.588  52.492  131.082 1.00 13.79 ? 199  ARG D C     1 
ATOM   9151  O  O     . ARG L  3 199 ? 70.874  53.479  131.270 1.00 14.90 ? 199  ARG D O     1 
ATOM   9152  C  CB    . ARG L  3 199 ? 71.437  51.301  128.901 1.00 15.06 ? 199  ARG D CB    1 
ATOM   9153  C  CG    . ARG L  3 199 ? 71.901  51.161  127.456 1.00 19.62 ? 199  ARG D CG    1 
ATOM   9154  C  CD    . ARG L  3 199 ? 70.929  50.322  126.655 1.00 18.93 ? 199  ARG D CD    1 
ATOM   9155  N  NE    . ARG L  3 199 ? 71.508  49.865  125.385 1.00 19.18 ? 199  ARG D NE    1 
ATOM   9156  C  CZ    . ARG L  3 199 ? 71.390  50.521  124.239 1.00 22.11 ? 199  ARG D CZ    1 
ATOM   9157  N  NH1   . ARG L  3 199 ? 70.716  51.661  124.202 1.00 21.99 ? 199  ARG D NH1   1 
ATOM   9158  N  NH2   . ARG L  3 199 ? 71.923  50.031  123.126 1.00 21.81 ? 199  ARG D NH2   1 
ATOM   9159  N  N     . SER L  3 200 ? 71.822  51.581  132.033 1.00 15.50 ? 200  SER D N     1 
ATOM   9160  C  CA    . SER L  3 200 ? 71.182  51.765  133.335 1.00 15.65 ? 200  SER D CA    1 
ATOM   9161  C  C     . SER L  3 200 ? 71.768  52.973  134.074 1.00 16.02 ? 200  SER D C     1 
ATOM   9162  O  O     . SER L  3 200 ? 71.035  53.716  134.741 1.00 17.41 ? 200  SER D O     1 
ATOM   9163  C  CB    . SER L  3 200 ? 71.257  50.474  134.176 1.00 15.94 ? 200  SER D CB    1 
ATOM   9164  O  OG    . SER L  3 200 ? 72.588  50.064  134.380 1.00 17.05 ? 200  SER D OG    1 
ATOM   9165  N  N     . GLU L  3 201 ? 73.074  53.201  133.940 1.00 16.61 ? 201  GLU D N     1 
ATOM   9166  C  CA    . GLU L  3 201 ? 73.678  54.358  134.587 1.00 15.27 ? 201  GLU D CA    1 
ATOM   9167  C  C     . GLU L  3 201 ? 73.172  55.644  133.925 1.00 15.30 ? 201  GLU D C     1 
ATOM   9168  O  O     . GLU L  3 201 ? 72.892  56.630  134.613 1.00 17.01 ? 201  GLU D O     1 
ATOM   9169  C  CB    . GLU L  3 201 ? 75.203  54.237  134.574 1.00 20.01 ? 201  GLU D CB    1 
ATOM   9170  C  CG    . GLU L  3 201 ? 75.628  53.193  135.611 1.00 19.66 ? 201  GLU D CG    1 
ATOM   9171  C  CD    . GLU L  3 201 ? 77.122  52.925  135.667 1.00 25.94 ? 201  GLU D CD    1 
ATOM   9172  O  OE1   . GLU L  3 201 ? 77.917  53.903  135.658 1.00 23.65 ? 201  GLU D OE1   1 
ATOM   9173  O  OE2   . GLU L  3 201 ? 77.485  51.729  135.748 1.00 27.05 ? 201  GLU D OE2   1 
ATOM   9174  N  N     . GLY L  3 202 ? 73.008  55.629  132.602 1.00 14.29 ? 202  GLY D N     1 
ATOM   9175  C  CA    . GLY L  3 202 ? 72.474  56.809  131.933 1.00 14.75 ? 202  GLY D CA    1 
ATOM   9176  C  C     . GLY L  3 202 ? 71.039  57.119  132.379 1.00 14.63 ? 202  GLY D C     1 
ATOM   9177  O  O     . GLY L  3 202 ? 70.710  58.284  132.649 1.00 16.12 ? 202  GLY D O     1 
ATOM   9178  N  N     . LEU L  3 203 ? 70.212  56.087  132.502 1.00 14.12 ? 203  LEU D N     1 
ATOM   9179  C  CA    . LEU L  3 203 ? 68.815  56.260  132.906 1.00 17.13 ? 203  LEU D CA    1 
ATOM   9180  C  C     . LEU L  3 203 ? 68.761  56.849  134.312 1.00 16.17 ? 203  LEU D C     1 
ATOM   9181  O  O     . LEU L  3 203 ? 67.906  57.700  134.604 1.00 15.96 ? 203  LEU D O     1 
ATOM   9182  C  CB    . LEU L  3 203 ? 68.082  54.922  132.870 1.00 19.46 ? 203  LEU D CB    1 
ATOM   9183  C  CG    . LEU L  3 203 ? 66.558  54.941  133.035 1.00 31.02 ? 203  LEU D CG    1 
ATOM   9184  C  CD1   . LEU L  3 203 ? 65.939  55.823  131.947 1.00 35.01 ? 203  LEU D CD1   1 
ATOM   9185  C  CD2   . LEU L  3 203 ? 66.024  53.514  132.943 1.00 33.90 ? 203  LEU D CD2   1 
ATOM   9186  N  N     . ASN L  3 204 ? 69.641  56.403  135.202 1.00 18.54 ? 204  ASN D N     1 
ATOM   9187  C  CA    . ASN L  3 204 ? 69.625  56.989  136.539 1.00 16.16 ? 204  ASN D CA    1 
ATOM   9188  C  C     . ASN L  3 204 ? 69.954  58.486  136.518 1.00 16.14 ? 204  ASN D C     1 
ATOM   9189  O  O     . ASN L  3 204 ? 69.356  59.261  137.261 1.00 16.88 ? 204  ASN D O     1 
ATOM   9190  C  CB    . ASN L  3 204 ? 70.561  56.216  137.458 1.00 23.11 ? 204  ASN D CB    1 
ATOM   9191  C  CG    . ASN L  3 204 ? 69.907  54.946  137.980 1.00 31.83 ? 204  ASN D CG    1 
ATOM   9192  O  OD1   . ASN L  3 204 ? 68.709  54.955  138.293 1.00 36.42 ? 204  ASN D OD1   1 
ATOM   9193  N  ND2   . ASN L  3 204 ? 70.672  53.856  138.081 1.00 31.90 ? 204  ASN D ND2   1 
ATOM   9194  N  N     . LEU L  3 205 ? 70.874  58.915  135.641 1.00 16.14 ? 205  LEU D N     1 
ATOM   9195  C  CA    . LEU L  3 205 ? 71.210  60.337  135.558 1.00 12.80 ? 205  LEU D CA    1 
ATOM   9196  C  C     . LEU L  3 205 ? 70.018  61.113  135.011 1.00 13.07 ? 205  LEU D C     1 
ATOM   9197  O  O     . LEU L  3 205 ? 69.735  62.235  135.415 1.00 15.47 ? 205  LEU D O     1 
ATOM   9198  C  CB    . LEU L  3 205 ? 72.443  60.556  134.666 1.00 14.98 ? 205  LEU D CB    1 
ATOM   9199  C  CG    . LEU L  3 205 ? 73.710  59.995  135.320 1.00 16.25 ? 205  LEU D CG    1 
ATOM   9200  C  CD1   . LEU L  3 205 ? 74.821  60.047  134.263 1.00 19.97 ? 205  LEU D CD1   1 
ATOM   9201  C  CD2   . LEU L  3 205 ? 74.103  60.793  136.562 1.00 18.62 ? 205  LEU D CD2   1 
ATOM   9202  N  N     . VAL L  3 206 ? 69.305  60.494  134.075 1.00 13.60 ? 206  VAL D N     1 
ATOM   9203  C  CA    . VAL L  3 206 ? 68.139  61.140  133.505 1.00 13.35 ? 206  VAL D CA    1 
ATOM   9204  C  C     . VAL L  3 206 ? 67.015  61.306  134.538 1.00 15.36 ? 206  VAL D C     1 
ATOM   9205  O  O     . VAL L  3 206 ? 66.471  62.401  134.737 1.00 17.19 ? 206  VAL D O     1 
ATOM   9206  C  CB    . VAL L  3 206 ? 67.575  60.293  132.330 1.00 14.93 ? 206  VAL D CB    1 
ATOM   9207  C  CG1   . VAL L  3 206 ? 66.174  60.819  131.930 1.00 19.89 ? 206  VAL D CG1   1 
ATOM   9208  C  CG2   . VAL L  3 206 ? 68.568  60.295  131.147 1.00 15.99 ? 206  VAL D CG2   1 
ATOM   9209  N  N     . ARG L  3 207 ? 66.685  60.203  135.208 1.00 15.01 ? 207  ARG D N     1 
ATOM   9210  C  CA    . ARG L  3 207 ? 65.534  60.192  136.117 1.00 15.33 ? 207  ARG D CA    1 
ATOM   9211  C  C     . ARG L  3 207 ? 65.657  61.018  137.386 1.00 18.35 ? 207  ARG D C     1 
ATOM   9212  O  O     . ARG L  3 207 ? 64.649  61.506  137.917 1.00 19.02 ? 207  ARG D O     1 
ATOM   9213  C  CB    . ARG L  3 207 ? 65.217  58.730  136.495 1.00 18.35 ? 207  ARG D CB    1 
ATOM   9214  C  CG    . ARG L  3 207 ? 64.862  57.856  135.300 1.00 27.87 ? 207  ARG D CG    1 
ATOM   9215  C  CD    . ARG L  3 207 ? 64.609  56.387  135.649 1.00 39.23 ? 207  ARG D CD    1 
ATOM   9216  N  NE    . ARG L  3 207 ? 63.966  55.713  134.517 1.00 44.89 ? 207  ARG D NE    1 
ATOM   9217  C  CZ    . ARG L  3 207 ? 63.652  54.420  134.469 1.00 51.16 ? 207  ARG D CZ    1 
ATOM   9218  N  NH1   . ARG L  3 207 ? 63.919  53.618  135.496 1.00 50.89 ? 207  ARG D NH1   1 
ATOM   9219  N  NH2   . ARG L  3 207 ? 63.064  53.930  133.380 1.00 50.69 ? 207  ARG D NH2   1 
ATOM   9220  N  N     . ASN L  3 208 ? 66.885  61.179  137.862 1.00 17.99 ? 208  ASN D N     1 
ATOM   9221  C  CA    . ASN L  3 208 ? 67.122  61.867  139.130 1.00 18.03 ? 208  ASN D CA    1 
ATOM   9222  C  C     . ASN L  3 208 ? 67.667  63.273  139.102 1.00 20.73 ? 208  ASN D C     1 
ATOM   9223  O  O     . ASN L  3 208 ? 67.958  63.867  140.153 1.00 20.29 ? 208  ASN D O     1 
ATOM   9224  C  CB    . ASN L  3 208 ? 68.038  60.997  139.990 1.00 17.03 ? 208  ASN D CB    1 
ATOM   9225  C  CG    . ASN L  3 208 ? 67.376  59.707  140.397 1.00 26.48 ? 208  ASN D CG    1 
ATOM   9226  O  OD1   . ASN L  3 208 ? 66.326  59.714  141.048 1.00 31.94 ? 208  ASN D OD1   1 
ATOM   9227  N  ND2   . ASN L  3 208 ? 67.961  58.594  140.010 1.00 24.81 ? 208  ASN D ND2   1 
ATOM   9228  N  N     . ARG L  3 209 ? 67.782  63.855  137.916 1.00 16.21 ? 209  ARG D N     1 
ATOM   9229  C  CA    . ARG L  3 209 ? 68.350  65.183  137.825 1.00 16.74 ? 209  ARG D CA    1 
ATOM   9230  C  C     . ARG L  3 209 ? 67.470  66.340  138.258 1.00 17.64 ? 209  ARG D C     1 
ATOM   9231  O  O     . ARG L  3 209 ? 66.245  66.295  138.130 1.00 17.46 ? 209  ARG D O     1 
ATOM   9232  C  CB    . ARG L  3 209 ? 68.761  65.467  136.377 1.00 15.86 ? 209  ARG D CB    1 
ATOM   9233  C  CG    . ARG L  3 209 ? 67.566  65.848  135.484 1.00 18.56 ? 209  ARG D CG    1 
ATOM   9234  C  CD    . ARG L  3 209 ? 68.002  66.049  134.037 1.00 17.89 ? 209  ARG D CD    1 
ATOM   9235  N  NE    . ARG L  3 209 ? 66.917  66.621  133.224 1.00 14.58 ? 209  ARG D NE    1 
ATOM   9236  C  CZ    . ARG L  3 209 ? 65.890  65.942  132.710 1.00 13.37 ? 209  ARG D CZ    1 
ATOM   9237  N  NH1   . ARG L  3 209 ? 65.764  64.627  132.887 1.00 15.51 ? 209  ARG D NH1   1 
ATOM   9238  N  NH2   . ARG L  3 209 ? 64.941  66.605  132.047 1.00 14.72 ? 209  ARG D NH2   1 
ATOM   9239  N  N     . LYS L  3 210 ? 68.136  67.377  138.765 1.00 19.34 ? 210  LYS D N     1 
ATOM   9240  C  CA    . LYS L  3 210 ? 67.494  68.646  139.055 1.00 20.24 ? 210  LYS D CA    1 
ATOM   9241  C  C     . LYS L  3 210 ? 68.407  69.599  138.277 1.00 23.57 ? 210  LYS D C     1 
ATOM   9242  O  O     . LYS L  3 210 ? 69.541  69.838  138.671 1.00 28.30 ? 210  LYS D O     1 
ATOM   9243  C  CB    . LYS L  3 210 ? 67.491  68.964  140.557 1.00 21.69 ? 210  LYS D CB    1 
ATOM   9244  C  CG    . LYS L  3 210 ? 66.594  68.033  141.322 1.00 16.28 ? 210  LYS D CG    1 
ATOM   9245  C  CD    . LYS L  3 210 ? 66.350  68.535  142.752 1.00 20.99 ? 210  LYS D CD    1 
ATOM   9246  C  CE    . LYS L  3 210 ? 65.577  67.507  143.538 1.00 21.25 ? 210  LYS D CE    1 
ATOM   9247  N  NZ    . LYS L  3 210 ? 65.466  67.951  144.963 1.00 28.72 ? 210  LYS D NZ    1 
ATOM   9248  N  N     . GLY L  3 211 ? 67.934  70.119  137.152 1.00 20.55 ? 211  GLY D N     1 
ATOM   9249  C  CA    . GLY L  3 211 ? 68.753  71.003  136.340 1.00 22.21 ? 211  GLY D CA    1 
ATOM   9250  C  C     . GLY L  3 211 ? 69.006  70.316  135.000 1.00 17.32 ? 211  GLY D C     1 
ATOM   9251  O  O     . GLY L  3 211 ? 68.411  69.272  134.758 1.00 16.99 ? 211  GLY D O     1 
ATOM   9252  N  N     . ARG L  3 212 ? 69.887  70.876  134.161 1.00 19.14 ? 212  ARG D N     1 
ATOM   9253  C  CA    . ARG L  3 212 ? 70.169  70.281  132.840 1.00 16.38 ? 212  ARG D CA    1 
ATOM   9254  C  C     . ARG L  3 212 ? 70.912  68.948  132.959 1.00 18.90 ? 212  ARG D C     1 
ATOM   9255  O  O     . ARG L  3 212 ? 71.819  68.793  133.779 1.00 22.38 ? 212  ARG D O     1 
ATOM   9256  C  CB    . ARG L  3 212 ? 70.980  71.241  131.944 1.00 17.48 ? 212  ARG D CB    1 
ATOM   9257  C  CG    . ARG L  3 212 ? 71.072  70.751  130.465 1.00 17.96 ? 212  ARG D CG    1 
ATOM   9258  C  CD    . ARG L  3 212 ? 71.832  71.676  129.531 1.00 17.89 ? 212  ARG D CD    1 
ATOM   9259  N  NE    . ARG L  3 212 ? 71.778  71.116  128.174 1.00 20.85 ? 212  ARG D NE    1 
ATOM   9260  C  CZ    . ARG L  3 212 ? 72.393  71.610  127.098 1.00 23.74 ? 212  ARG D CZ    1 
ATOM   9261  N  NH1   . ARG L  3 212 ? 73.143  72.709  127.181 1.00 23.77 ? 212  ARG D NH1   1 
ATOM   9262  N  NH2   . ARG L  3 212 ? 72.260  70.987  125.928 1.00 21.50 ? 212  ARG D NH2   1 
ATOM   9263  N  N     . LEU L  3 213 ? 70.497  67.989  132.144 1.00 14.95 ? 213  LEU D N     1 
ATOM   9264  C  CA    . LEU L  3 213 ? 71.130  66.683  132.126 1.00 15.49 ? 213  LEU D CA    1 
ATOM   9265  C  C     . LEU L  3 213 ? 72.582  66.826  131.683 1.00 15.40 ? 213  LEU D C     1 
ATOM   9266  O  O     . LEU L  3 213 ? 72.872  67.576  130.756 1.00 16.30 ? 213  LEU D O     1 
ATOM   9267  C  CB    . LEU L  3 213 ? 70.399  65.774  131.126 1.00 13.95 ? 213  LEU D CB    1 
ATOM   9268  C  CG    . LEU L  3 213 ? 70.873  64.308  131.103 1.00 13.61 ? 213  LEU D CG    1 
ATOM   9269  C  CD1   . LEU L  3 213 ? 70.421  63.611  132.405 1.00 16.02 ? 213  LEU D CD1   1 
ATOM   9270  C  CD2   . LEU L  3 213 ? 70.255  63.577  129.882 1.00 14.31 ? 213  LEU D CD2   1 
ATOM   9271  N  N     . PRO L  3 214 ? 73.517  66.144  132.360 1.00 14.40 ? 214  PRO D N     1 
ATOM   9272  C  CA    . PRO L  3 214 ? 74.915  66.265  131.915 1.00 14.95 ? 214  PRO D CA    1 
ATOM   9273  C  C     . PRO L  3 214 ? 75.048  65.546  130.560 1.00 12.79 ? 214  PRO D C     1 
ATOM   9274  O  O     . PRO L  3 214 ? 74.139  64.834  130.110 1.00 13.83 ? 214  PRO D O     1 
ATOM   9275  C  CB    . PRO L  3 214 ? 75.695  65.453  132.954 1.00 19.13 ? 214  PRO D CB    1 
ATOM   9276  C  CG    . PRO L  3 214 ? 74.820  65.550  134.198 1.00 22.63 ? 214  PRO D CG    1 
ATOM   9277  C  CD    . PRO L  3 214 ? 73.420  65.407  133.632 1.00 16.55 ? 214  PRO D CD    1 
ATOM   9278  N  N     . HIS L  3 215 ? 76.198  65.744  129.935 1.00 13.49 ? 215  HIS D N     1 
ATOM   9279  C  CA    . HIS L  3 215 ? 76.532  64.969  128.739 1.00 12.46 ? 215  HIS D CA    1 
ATOM   9280  C  C     . HIS L  3 215 ? 76.611  63.524  129.267 1.00 14.70 ? 215  HIS D C     1 
ATOM   9281  O  O     . HIS L  3 215 ? 77.122  63.295  130.373 1.00 13.81 ? 215  HIS D O     1 
ATOM   9282  C  CB    . HIS L  3 215 ? 77.920  65.359  128.255 1.00 13.33 ? 215  HIS D CB    1 
ATOM   9283  C  CG    . HIS L  3 215 ? 77.939  66.628  127.476 1.00 14.56 ? 215  HIS D CG    1 
ATOM   9284  N  ND1   . HIS L  3 215 ? 78.210  67.866  128.034 1.00 17.57 ? 215  HIS D ND1   1 
ATOM   9285  C  CD2   . HIS L  3 215 ? 77.711  66.844  126.166 1.00 10.90 ? 215  HIS D CD2   1 
ATOM   9286  C  CE1   . HIS L  3 215 ? 78.147  68.789  127.086 1.00 13.29 ? 215  HIS D CE1   1 
ATOM   9287  N  NE2   . HIS L  3 215 ? 77.843  68.192  125.945 1.00 19.50 ? 215  HIS D NE2   1 
ATOM   9288  N  N     . ILE L  3 216 ? 76.126  62.557  128.491 1.00 12.31 ? 216  ILE D N     1 
ATOM   9289  C  CA    . ILE L  3 216 ? 76.208  61.138  128.872 1.00 13.51 ? 216  ILE D CA    1 
ATOM   9290  C  C     . ILE L  3 216 ? 76.787  60.424  127.650 1.00 12.80 ? 216  ILE D C     1 
ATOM   9291  O  O     . ILE L  3 216 ? 76.089  60.244  126.654 1.00 12.64 ? 216  ILE D O     1 
ATOM   9292  C  CB    . ILE L  3 216 ? 74.835  60.557  129.186 1.00 12.10 ? 216  ILE D CB    1 
ATOM   9293  C  CG1   . ILE L  3 216 ? 74.196  61.338  130.343 1.00 15.89 ? 216  ILE D CG1   1 
ATOM   9294  C  CG2   . ILE L  3 216 ? 74.977  59.100  129.601 1.00 15.50 ? 216  ILE D CG2   1 
ATOM   9295  C  CD1   . ILE L  3 216 ? 72.775  60.852  130.694 1.00 16.80 ? 216  ILE D CD1   1 
ATOM   9296  N  N     . VAL L  3 217 ? 78.066  60.043  127.718 1.00 11.98 ? 217  VAL D N     1 
ATOM   9297  C  CA    . VAL L  3 217 ? 78.711  59.412  126.555 1.00 11.83 ? 217  VAL D CA    1 
ATOM   9298  C  C     . VAL L  3 217 ? 79.483  58.163  126.935 1.00 13.32 ? 217  VAL D C     1 
ATOM   9299  O  O     . VAL L  3 217 ? 79.711  57.905  128.113 1.00 13.19 ? 217  VAL D O     1 
ATOM   9300  C  CB    . VAL L  3 217 ? 79.687  60.391  125.866 1.00 14.16 ? 217  VAL D CB    1 
ATOM   9301  C  CG1   . VAL L  3 217 ? 78.933  61.658  125.448 1.00 13.72 ? 217  VAL D CG1   1 
ATOM   9302  C  CG2   . VAL L  3 217 ? 80.827  60.785  126.822 1.00 14.12 ? 217  VAL D CG2   1 
ATOM   9303  N  N     . VAL L  3 218 ? 79.847  57.369  125.928 1.00 11.76 ? 218  VAL D N     1 
ATOM   9304  C  CA    . VAL L  3 218 ? 80.629  56.160  126.159 1.00 13.57 ? 218  VAL D CA    1 
ATOM   9305  C  C     . VAL L  3 218 ? 81.822  56.198  125.221 1.00 14.42 ? 218  VAL D C     1 
ATOM   9306  O  O     . VAL L  3 218 ? 81.687  56.595  124.068 1.00 13.86 ? 218  VAL D O     1 
ATOM   9307  C  CB    . VAL L  3 218 ? 79.811  54.880  125.842 1.00 13.67 ? 218  VAL D CB    1 
ATOM   9308  C  CG1   . VAL L  3 218 ? 80.695  53.639  126.077 1.00 14.24 ? 218  VAL D CG1   1 
ATOM   9309  C  CG2   . VAL L  3 218 ? 78.550  54.825  126.703 1.00 13.70 ? 218  VAL D CG2   1 
ATOM   9310  N  N     . VAL L  3 219 ? 82.991  55.812  125.716 1.00 9.97  ? 219  VAL D N     1 
ATOM   9311  C  CA    . VAL L  3 219 ? 84.186  55.759  124.864 1.00 12.14 ? 219  VAL D CA    1 
ATOM   9312  C  C     . VAL L  3 219 ? 84.614  54.299  124.872 1.00 14.09 ? 219  VAL D C     1 
ATOM   9313  O  O     . VAL L  3 219 ? 84.658  53.660  125.940 1.00 14.00 ? 219  VAL D O     1 
ATOM   9314  C  CB    . VAL L  3 219 ? 85.350  56.612  125.427 1.00 13.04 ? 219  VAL D CB    1 
ATOM   9315  C  CG1   . VAL L  3 219 ? 86.586  56.469  124.484 1.00 14.15 ? 219  VAL D CG1   1 
ATOM   9316  C  CG2   . VAL L  3 219 ? 84.912  58.100  125.538 1.00 13.71 ? 219  VAL D CG2   1 
ATOM   9317  N  N     . THR L  3 220 ? 84.961  53.749  123.711 1.00 10.78 ? 220  THR D N     1 
ATOM   9318  C  CA    . THR L  3 220 ? 85.340  52.340  123.683 1.00 12.21 ? 220  THR D CA    1 
ATOM   9319  C  C     . THR L  3 220 ? 86.438  52.023  122.686 1.00 13.85 ? 220  THR D C     1 
ATOM   9320  O  O     . THR L  3 220 ? 86.635  52.754  121.705 1.00 13.34 ? 220  THR D O     1 
ATOM   9321  C  CB    . THR L  3 220 ? 84.077  51.435  123.371 1.00 13.08 ? 220  THR D CB    1 
ATOM   9322  O  OG1   . THR L  3 220 ? 84.423  50.052  123.482 1.00 12.68 ? 220  THR D OG1   1 
ATOM   9323  C  CG2   . THR L  3 220 ? 83.529  51.678  121.937 1.00 14.16 ? 220  THR D CG2   1 
ATOM   9324  N  N     . ALA L  3 221 ? 87.176  50.956  122.976 1.00 11.95 ? 221  ALA D N     1 
ATOM   9325  C  CA    . ALA L  3 221 ? 88.201  50.468  122.050 1.00 14.29 ? 221  ALA D CA    1 
ATOM   9326  C  C     . ALA L  3 221 ? 87.757  49.126  121.404 1.00 14.51 ? 221  ALA D C     1 
ATOM   9327  O  O     . ALA L  3 221 ? 88.562  48.445  120.752 1.00 15.14 ? 221  ALA D O     1 
ATOM   9328  C  CB    . ALA L  3 221 ? 89.575  50.297  122.779 1.00 13.80 ? 221  ALA D CB    1 
ATOM   9329  N  N     . GLU L  3 222 ? 86.494  48.746  121.592 1.00 13.34 ? 222  GLU D N     1 
ATOM   9330  C  CA    . GLU L  3 222 ? 85.964  47.501  121.018 1.00 11.89 ? 222  GLU D CA    1 
ATOM   9331  C  C     . GLU L  3 222 ? 86.159  47.540  119.491 1.00 12.34 ? 222  GLU D C     1 
ATOM   9332  O  O     . GLU L  3 222 ? 85.737  48.473  118.847 1.00 13.87 ? 222  GLU D O     1 
ATOM   9333  C  CB    . GLU L  3 222 ? 84.470  47.389  121.324 1.00 14.16 ? 222  GLU D CB    1 
ATOM   9334  C  CG    . GLU L  3 222 ? 83.768  46.279  120.535 1.00 14.39 ? 222  GLU D CG    1 
ATOM   9335  C  CD    . GLU L  3 222 ? 84.428  44.916  120.733 1.00 19.27 ? 222  GLU D CD    1 
ATOM   9336  O  OE1   . GLU L  3 222 ? 84.479  44.127  119.753 1.00 14.60 ? 222  GLU D OE1   1 
ATOM   9337  O  OE2   . GLU L  3 222 ? 84.885  44.627  121.860 1.00 13.09 ? 222  GLU D OE2   1 
ATOM   9338  N  N     . PRO L  3 223 ? 86.761  46.503  118.906 1.00 12.71 ? 223  PRO D N     1 
ATOM   9339  C  CA    . PRO L  3 223 ? 86.960  46.542  117.448 1.00 13.23 ? 223  PRO D CA    1 
ATOM   9340  C  C     . PRO L  3 223 ? 85.775  46.198  116.549 1.00 15.39 ? 223  PRO D C     1 
ATOM   9341  O  O     . PRO L  3 223 ? 85.704  46.687  115.426 1.00 15.89 ? 223  PRO D O     1 
ATOM   9342  C  CB    . PRO L  3 223 ? 88.125  45.566  117.223 1.00 15.42 ? 223  PRO D CB    1 
ATOM   9343  C  CG    . PRO L  3 223 ? 87.978  44.579  118.330 1.00 18.85 ? 223  PRO D CG    1 
ATOM   9344  C  CD    . PRO L  3 223 ? 87.578  45.452  119.537 1.00 13.43 ? 223  PRO D CD    1 
ATOM   9345  N  N     . THR L  3 224 ? 84.832  45.391  117.027 1.00 13.86 ? 224  THR D N     1 
ATOM   9346  C  CA    . THR L  3 224 ? 83.752  44.981  116.134 1.00 12.36 ? 224  THR D CA    1 
ATOM   9347  C  C     . THR L  3 224 ? 82.504  45.867  116.118 1.00 14.34 ? 224  THR D C     1 
ATOM   9348  O  O     . THR L  3 224 ? 81.980  46.251  117.182 1.00 14.07 ? 224  THR D O     1 
ATOM   9349  C  CB    . THR L  3 224 ? 83.283  43.509  116.403 1.00 15.74 ? 224  THR D CB    1 
ATOM   9350  O  OG1   . THR L  3 224 ? 82.575  43.403  117.659 1.00 16.08 ? 224  THR D OG1   1 
ATOM   9351  C  CG2   . THR L  3 224 ? 84.489  42.546  116.409 1.00 15.10 ? 224  THR D CG2   1 
ATOM   9352  N  N     . PRO L  3 225 ? 82.024  46.244  114.913 1.00 15.11 ? 225  PRO D N     1 
ATOM   9353  C  CA    . PRO L  3 225 ? 80.814  47.077  114.860 1.00 13.26 ? 225  PRO D CA    1 
ATOM   9354  C  C     . PRO L  3 225 ? 79.622  46.383  115.565 1.00 13.74 ? 225  PRO D C     1 
ATOM   9355  O  O     . PRO L  3 225 ? 78.780  47.045  116.193 1.00 14.99 ? 225  PRO D O     1 
ATOM   9356  C  CB    . PRO L  3 225 ? 80.574  47.244  113.341 1.00 16.37 ? 225  PRO D CB    1 
ATOM   9357  C  CG    . PRO L  3 225 ? 81.983  47.348  112.817 1.00 14.92 ? 225  PRO D CG    1 
ATOM   9358  C  CD    . PRO L  3 225 ? 82.707  46.211  113.597 1.00 15.88 ? 225  PRO D CD    1 
ATOM   9359  N  N     . SER L  3 226 ? 79.549  45.050  115.486 1.00 14.50 ? 226  SER D N     1 
ATOM   9360  C  CA    . SER L  3 226 ? 78.445  44.350  116.147 1.00 14.74 ? 226  SER D CA    1 
ATOM   9361  C  C     . SER L  3 226 ? 78.435  44.616  117.660 1.00 13.90 ? 226  SER D C     1 
ATOM   9362  O  O     . SER L  3 226 ? 77.391  44.959  118.215 1.00 14.62 ? 226  SER D O     1 
ATOM   9363  C  CB    . SER L  3 226 ? 78.508  42.843  115.852 1.00 17.52 ? 226  SER D CB    1 
ATOM   9364  O  OG    . SER L  3 226 ? 79.729  42.283  116.276 1.00 20.07 ? 226  SER D OG    1 
ATOM   9365  N  N     . ARG L  3 227 ? 79.583  44.475  118.319 1.00 14.83 ? 227  ARG D N     1 
ATOM   9366  C  CA    . ARG L  3 227 ? 79.603  44.724  119.765 1.00 12.92 ? 227  ARG D CA    1 
ATOM   9367  C  C     . ARG L  3 227 ? 79.427  46.202  120.105 1.00 14.73 ? 227  ARG D C     1 
ATOM   9368  O  O     . ARG L  3 227 ? 78.755  46.544  121.086 1.00 14.04 ? 227  ARG D O     1 
ATOM   9369  C  CB    . ARG L  3 227 ? 80.890  44.135  120.370 1.00 14.87 ? 227  ARG D CB    1 
ATOM   9370  C  CG    . ARG L  3 227 ? 80.753  42.601  120.532 1.00 12.37 ? 227  ARG D CG    1 
ATOM   9371  C  CD    . ARG L  3 227 ? 82.053  41.902  120.848 1.00 13.75 ? 227  ARG D CD    1 
ATOM   9372  N  NE    . ARG L  3 227 ? 81.788  40.522  121.284 1.00 14.16 ? 227  ARG D NE    1 
ATOM   9373  C  CZ    . ARG L  3 227 ? 82.648  39.509  121.171 1.00 16.37 ? 227  ARG D CZ    1 
ATOM   9374  N  NH1   . ARG L  3 227 ? 83.845  39.693  120.627 1.00 15.88 ? 227  ARG D NH1   1 
ATOM   9375  N  NH2   . ARG L  3 227 ? 82.312  38.301  121.629 1.00 15.12 ? 227  ARG D NH2   1 
ATOM   9376  N  N     . ILE L  3 228 ? 79.993  47.081  119.286 1.00 14.10 ? 228  ILE D N     1 
ATOM   9377  C  CA    . ILE L  3 228 ? 79.823  48.514  119.509 1.00 12.89 ? 228  ILE D CA    1 
ATOM   9378  C  C     . ILE L  3 228 ? 78.324  48.828  119.423 1.00 13.52 ? 228  ILE D C     1 
ATOM   9379  O  O     . ILE L  3 228 ? 77.787  49.607  120.216 1.00 13.85 ? 228  ILE D O     1 
ATOM   9380  C  CB    . ILE L  3 228 ? 80.569  49.323  118.415 1.00 10.86 ? 228  ILE D CB    1 
ATOM   9381  C  CG1   . ILE L  3 228 ? 82.087  49.134  118.571 1.00 11.68 ? 228  ILE D CG1   1 
ATOM   9382  C  CG2   . ILE L  3 228 ? 80.187  50.819  118.526 1.00 14.59 ? 228  ILE D CG2   1 
ATOM   9383  C  CD1   . ILE L  3 228 ? 82.880  49.644  117.348 1.00 14.51 ? 228  ILE D CD1   1 
ATOM   9384  N  N     . SER L  3 229 ? 77.623  48.176  118.497 1.00 11.90 ? 229  SER D N     1 
ATOM   9385  C  CA    . SER L  3 229 ? 76.205  48.461  118.308 1.00 12.22 ? 229  SER D CA    1 
ATOM   9386  C  C     . SER L  3 229 ? 75.323  48.091  119.514 1.00 12.39 ? 229  SER D C     1 
ATOM   9387  O  O     . SER L  3 229 ? 74.240  48.657  119.674 1.00 13.68 ? 229  SER D O     1 
ATOM   9388  C  CB    . SER L  3 229 ? 75.711  47.763  116.997 1.00 14.98 ? 229  SER D CB    1 
ATOM   9389  O  OG    . SER L  3 229 ? 75.413  46.386  117.234 1.00 16.62 ? 229  SER D OG    1 
ATOM   9390  N  N     . SER L  3 230 ? 75.792  47.153  120.346 1.00 13.91 ? 230  SER D N     1 
ATOM   9391  C  CA    . SER L  3 230 ? 75.045  46.745  121.527 1.00 14.78 ? 230  SER D CA    1 
ATOM   9392  C  C     . SER L  3 230 ? 74.854  47.909  122.509 1.00 16.05 ? 230  SER D C     1 
ATOM   9393  O  O     . SER L  3 230 ? 73.977  47.856  123.375 1.00 15.57 ? 230  SER D O     1 
ATOM   9394  C  CB    . SER L  3 230 ? 75.732  45.528  122.218 1.00 15.88 ? 230  SER D CB    1 
ATOM   9395  O  OG    . SER L  3 230 ? 76.897  45.886  122.941 1.00 17.13 ? 230  SER D OG    1 
ATOM   9396  N  N     . ILE L  3 231 ? 75.656  48.963  122.389 1.00 14.66 ? 231  ILE D N     1 
ATOM   9397  C  CA    . ILE L  3 231 ? 75.466  50.140  123.256 1.00 15.68 ? 231  ILE D CA    1 
ATOM   9398  C  C     . ILE L  3 231 ? 75.207  51.424  122.430 1.00 15.05 ? 231  ILE D C     1 
ATOM   9399  O  O     . ILE L  3 231 ? 74.532  52.342  122.892 1.00 15.37 ? 231  ILE D O     1 
ATOM   9400  C  CB    . ILE L  3 231 ? 76.690  50.341  124.223 1.00 17.37 ? 231  ILE D CB    1 
ATOM   9401  C  CG1   . ILE L  3 231 ? 76.399  51.466  125.223 1.00 22.07 ? 231  ILE D CG1   1 
ATOM   9402  C  CG2   . ILE L  3 231 ? 77.957  50.622  123.444 1.00 17.68 ? 231  ILE D CG2   1 
ATOM   9403  C  CD1   . ILE L  3 231 ? 75.108  51.192  126.058 1.00 23.64 ? 231  ILE D CD1   1 
ATOM   9404  N  N     . ALA L  3 232 ? 75.660  51.460  121.175 1.00 12.61 ? 232  ALA D N     1 
ATOM   9405  C  CA    . ALA L  3 232 ? 75.468  52.669  120.377 1.00 13.32 ? 232  ALA D CA    1 
ATOM   9406  C  C     . ALA L  3 232 ? 74.080  52.808  119.748 1.00 15.39 ? 232  ALA D C     1 
ATOM   9407  O  O     . ALA L  3 232 ? 73.580  53.923  119.587 1.00 14.20 ? 232  ALA D O     1 
ATOM   9408  C  CB    . ALA L  3 232 ? 76.523  52.734  119.289 1.00 14.24 ? 232  ALA D CB    1 
ATOM   9409  N  N     . LEU L  3 233 ? 73.467  51.694  119.349 1.00 16.30 ? 233  LEU D N     1 
ATOM   9410  C  CA    . LEU L  3 233 ? 72.141  51.801  118.738 1.00 17.85 ? 233  LEU D CA    1 
ATOM   9411  C  C     . LEU L  3 233 ? 71.079  52.113  119.775 1.00 16.63 ? 233  LEU D C     1 
ATOM   9412  O  O     . LEU L  3 233 ? 71.180  51.718  120.922 1.00 19.35 ? 233  LEU D O     1 
ATOM   9413  C  CB    . LEU L  3 233 ? 71.779  50.515  117.987 1.00 18.01 ? 233  LEU D CB    1 
ATOM   9414  C  CG    . LEU L  3 233 ? 72.656  50.197  116.764 1.00 16.87 ? 233  LEU D CG    1 
ATOM   9415  C  CD1   . LEU L  3 233 ? 72.314  48.790  116.261 1.00 19.67 ? 233  LEU D CD1   1 
ATOM   9416  C  CD2   . LEU L  3 233 ? 72.451  51.228  115.678 1.00 21.14 ? 233  LEU D CD2   1 
ATOM   9417  N  N     . GLY L  3 234 ? 70.054  52.830  119.340 1.00 19.43 ? 234  GLY D N     1 
ATOM   9418  C  CA    . GLY L  3 234 ? 68.973  53.189  120.220 1.00 21.00 ? 234  GLY D CA    1 
ATOM   9419  C  C     . GLY L  3 234 ? 69.273  54.574  120.746 1.00 21.60 ? 234  GLY D C     1 
ATOM   9420  O  O     . GLY L  3 234 ? 70.407  55.060  120.620 1.00 20.60 ? 234  GLY D O     1 
ATOM   9421  N  N     . THR L  3 235 ? 68.249  55.221  121.291 1.00 19.25 ? 235  THR D N     1 
ATOM   9422  C  CA    . THR L  3 235 ? 68.405  56.544  121.862 1.00 17.92 ? 235  THR D CA    1 
ATOM   9423  C  C     . THR L  3 235 ? 67.672  56.606  123.190 1.00 17.90 ? 235  THR D C     1 
ATOM   9424  O  O     . THR L  3 235 ? 66.825  55.746  123.513 1.00 20.79 ? 235  THR D O     1 
ATOM   9425  C  CB    . THR L  3 235 ? 67.800  57.670  120.925 1.00 17.57 ? 235  THR D CB    1 
ATOM   9426  O  OG1   . THR L  3 235 ? 66.424  57.361  120.632 1.00 18.04 ? 235  THR D OG1   1 
ATOM   9427  C  CG2   . THR L  3 235 ? 68.585  57.781  119.599 1.00 19.01 ? 235  THR D CG2   1 
ATOM   9428  N  N     . GLY L  3 236 ? 68.022  57.610  123.982 1.00 17.78 ? 236  GLY D N     1 
ATOM   9429  C  CA    . GLY L  3 236 ? 67.332  57.818  125.240 1.00 16.62 ? 236  GLY D CA    1 
ATOM   9430  C  C     . GLY L  3 236 ? 68.173  57.751  126.495 1.00 15.74 ? 236  GLY D C     1 
ATOM   9431  O  O     . GLY L  3 236 ? 67.903  58.459  127.475 1.00 17.67 ? 236  GLY D O     1 
ATOM   9432  N  N     . GLU L  3 237 ? 69.207  56.913  126.450 1.00 14.62 ? 237  GLU D N     1 
ATOM   9433  C  CA    . GLU L  3 237 ? 70.110  56.726  127.571 1.00 17.40 ? 237  GLU D CA    1 
ATOM   9434  C  C     . GLU L  3 237 ? 71.476  57.350  127.303 1.00 14.59 ? 237  GLU D C     1 
ATOM   9435  O  O     . GLU L  3 237 ? 72.019  58.093  128.135 1.00 16.42 ? 237  GLU D O     1 
ATOM   9436  C  CB    . GLU L  3 237 ? 70.376  55.235  127.819 1.00 17.51 ? 237  GLU D CB    1 
ATOM   9437  C  CG    . GLU L  3 237 ? 69.181  54.367  128.144 1.00 26.18 ? 237  GLU D CG    1 
ATOM   9438  C  CD    . GLU L  3 237 ? 68.528  53.724  126.928 1.00 29.84 ? 237  GLU D CD    1 
ATOM   9439  O  OE1   . GLU L  3 237 ? 69.209  53.388  125.910 1.00 22.76 ? 237  GLU D OE1   1 
ATOM   9440  O  OE2   . GLU L  3 237 ? 67.302  53.530  127.012 1.00 34.42 ? 237  GLU D OE2   1 
ATOM   9441  N  N     . ILE L  3 238 ? 72.031  57.043  126.138 1.00 14.04 ? 238  ILE D N     1 
ATOM   9442  C  CA    . ILE L  3 238 ? 73.372  57.472  125.750 1.00 13.31 ? 238  ILE D CA    1 
ATOM   9443  C  C     . ILE L  3 238 ? 73.337  58.551  124.680 1.00 13.44 ? 238  ILE D C     1 
ATOM   9444  O  O     . ILE L  3 238 ? 72.667  58.381  123.661 1.00 14.33 ? 238  ILE D O     1 
ATOM   9445  C  CB    . ILE L  3 238 ? 74.128  56.248  125.225 1.00 14.83 ? 238  ILE D CB    1 
ATOM   9446  C  CG1   . ILE L  3 238 ? 74.147  55.201  126.350 1.00 18.94 ? 238  ILE D CG1   1 
ATOM   9447  C  CG2   . ILE L  3 238 ? 75.556  56.607  124.780 1.00 14.95 ? 238  ILE D CG2   1 
ATOM   9448  C  CD1   . ILE L  3 238 ? 74.720  53.954  125.907 1.00 25.59 ? 238  ILE D CD1   1 
ATOM   9449  N  N     . ASP L  3 239 ? 74.042  59.649  124.901 1.00 11.96 ? 239  ASP D N     1 
ATOM   9450  C  CA    . ASP L  3 239 ? 74.029  60.735  123.894 1.00 12.21 ? 239  ASP D CA    1 
ATOM   9451  C  C     . ASP L  3 239 ? 74.685  60.274  122.585 1.00 13.84 ? 239  ASP D C     1 
ATOM   9452  O  O     . ASP L  3 239 ? 74.177  60.542  121.494 1.00 12.35 ? 239  ASP D O     1 
ATOM   9453  C  CB    . ASP L  3 239 ? 74.789  61.970  124.391 1.00 12.37 ? 239  ASP D CB    1 
ATOM   9454  C  CG    . ASP L  3 239 ? 74.166  62.603  125.638 1.00 12.05 ? 239  ASP D CG    1 
ATOM   9455  O  OD1   . ASP L  3 239 ? 73.079  62.166  126.074 1.00 15.10 ? 239  ASP D OD1   1 
ATOM   9456  O  OD2   . ASP L  3 239 ? 74.775  63.560  126.152 1.00 14.07 ? 239  ASP D OD2   1 
ATOM   9457  N  N     . CYS L  3 240 ? 75.841  59.634  122.724 1.00 12.33 ? 240  CYS D N     1 
ATOM   9458  C  CA    . CYS L  3 240 ? 76.639  59.173  121.590 1.00 12.04 ? 240  CYS D CA    1 
ATOM   9459  C  C     . CYS L  3 240 ? 77.792  58.313  122.111 1.00 13.61 ? 240  CYS D C     1 
ATOM   9460  O  O     . CYS L  3 240 ? 78.180  58.419  123.284 1.00 12.76 ? 240  CYS D O     1 
ATOM   9461  C  CB    . CYS L  3 240 ? 77.212  60.404  120.862 1.00 10.30 ? 240  CYS D CB    1 
ATOM   9462  S  SG    . CYS L  3 240 ? 77.875  60.070  119.198 1.00 14.67 ? 240  CYS D SG    1 
ATOM   9463  N  N     . VAL L  3 241 ? 78.331  57.465  121.240 1.00 11.13 ? 241  VAL D N     1 
ATOM   9464  C  CA    . VAL L  3 241 ? 79.489  56.631  121.554 1.00 10.98 ? 241  VAL D CA    1 
ATOM   9465  C  C     . VAL L  3 241 ? 80.660  57.133  120.726 1.00 13.88 ? 241  VAL D C     1 
ATOM   9466  O  O     . VAL L  3 241 ? 80.476  57.584  119.580 1.00 11.96 ? 241  VAL D O     1 
ATOM   9467  C  CB    . VAL L  3 241 ? 79.188  55.138  121.239 1.00 11.55 ? 241  VAL D CB    1 
ATOM   9468  C  CG1   . VAL L  3 241 ? 80.425  54.255  121.493 1.00 12.06 ? 241  VAL D CG1   1 
ATOM   9469  C  CG2   . VAL L  3 241 ? 77.991  54.697  122.104 1.00 13.91 ? 241  VAL D CG2   1 
ATOM   9470  N  N     . TYR L  3 242 ? 81.859  57.070  121.311 1.00 12.34 ? 242  TYR D N     1 
ATOM   9471  C  CA    . TYR L  3 242 ? 83.084  57.548  120.662 1.00 10.59 ? 242  TYR D CA    1 
ATOM   9472  C  C     . TYR L  3 242 ? 84.086  56.406  120.599 1.00 15.50 ? 242  TYR D C     1 
ATOM   9473  O  O     . TYR L  3 242 ? 84.393  55.783  121.604 1.00 13.53 ? 242  TYR D O     1 
ATOM   9474  C  CB    . TYR L  3 242 ? 83.673  58.719  121.462 1.00 13.28 ? 242  TYR D CB    1 
ATOM   9475  C  CG    . TYR L  3 242 ? 82.726  59.919  121.511 1.00 12.25 ? 242  TYR D CG    1 
ATOM   9476  C  CD1   . TYR L  3 242 ? 81.634  59.934  122.375 1.00 10.35 ? 242  TYR D CD1   1 
ATOM   9477  C  CD2   . TYR L  3 242 ? 82.870  60.988  120.617 1.00 14.61 ? 242  TYR D CD2   1 
ATOM   9478  C  CE1   . TYR L  3 242 ? 80.694  60.961  122.353 1.00 11.12 ? 242  TYR D CE1   1 
ATOM   9479  C  CE2   . TYR L  3 242 ? 81.951  62.029  120.577 1.00 11.82 ? 242  TYR D CE2   1 
ATOM   9480  C  CZ    . TYR L  3 242 ? 80.855  62.016  121.447 1.00 15.26 ? 242  TYR D CZ    1 
ATOM   9481  O  OH    . TYR L  3 242 ? 79.933  63.037  121.417 1.00 14.24 ? 242  TYR D OH    1 
ATOM   9482  N  N     . HIS L  3 243 ? 84.576  56.109  119.404 1.00 10.96 ? 243  HIS D N     1 
ATOM   9483  C  CA    . HIS L  3 243 ? 85.511  55.012  119.239 1.00 11.27 ? 243  HIS D CA    1 
ATOM   9484  C  C     . HIS L  3 243 ? 86.951  55.492  119.333 1.00 11.36 ? 243  HIS D C     1 
ATOM   9485  O  O     . HIS L  3 243 ? 87.291  56.553  118.800 1.00 13.52 ? 243  HIS D O     1 
ATOM   9486  C  CB    . HIS L  3 243 ? 85.256  54.330  117.883 1.00 10.87 ? 243  HIS D CB    1 
ATOM   9487  C  CG    . HIS L  3 243 ? 85.957  53.014  117.737 1.00 11.82 ? 243  HIS D CG    1 
ATOM   9488  N  ND1   . HIS L  3 243 ? 87.219  52.891  117.192 1.00 14.11 ? 243  HIS D ND1   1 
ATOM   9489  C  CD2   . HIS L  3 243 ? 85.587  51.763  118.124 1.00 12.19 ? 243  HIS D CD2   1 
ATOM   9490  C  CE1   . HIS L  3 243 ? 87.597  51.623  117.249 1.00 14.12 ? 243  HIS D CE1   1 
ATOM   9491  N  NE2   . HIS L  3 243 ? 86.627  50.921  117.811 1.00 13.11 ? 243  HIS D NE2   1 
ATOM   9492  N  N     . PHE L  3 244 ? 87.813  54.691  119.950 1.00 11.78 ? 244  PHE D N     1 
ATOM   9493  C  CA    . PHE L  3 244 ? 89.195  55.111  120.138 1.00 12.87 ? 244  PHE D CA    1 
ATOM   9494  C  C     . PHE L  3 244 ? 90.035  55.270  118.868 1.00 14.49 ? 244  PHE D C     1 
ATOM   9495  O  O     . PHE L  3 244 ? 91.049  55.955  118.895 1.00 15.84 ? 244  PHE D O     1 
ATOM   9496  C  CB    . PHE L  3 244 ? 89.922  54.163  121.121 1.00 16.04 ? 244  PHE D CB    1 
ATOM   9497  C  CG    . PHE L  3 244 ? 90.687  53.035  120.452 1.00 14.60 ? 244  PHE D CG    1 
ATOM   9498  C  CD1   . PHE L  3 244 ? 92.067  52.893  120.676 1.00 18.10 ? 244  PHE D CD1   1 
ATOM   9499  C  CD2   . PHE L  3 244 ? 90.032  52.096  119.656 1.00 12.76 ? 244  PHE D CD2   1 
ATOM   9500  C  CE1   . PHE L  3 244 ? 92.778  51.825  120.129 1.00 16.96 ? 244  PHE D CE1   1 
ATOM   9501  C  CE2   . PHE L  3 244 ? 90.731  51.027  119.104 1.00 15.48 ? 244  PHE D CE2   1 
ATOM   9502  C  CZ    . PHE L  3 244 ? 92.111  50.885  119.339 1.00 14.45 ? 244  PHE D CZ    1 
ATOM   9503  N  N     . ALA L  3 245 ? 89.608  54.656  117.768 1.00 14.80 ? 245  ALA D N     1 
ATOM   9504  C  CA    . ALA L  3 245 ? 90.369  54.717  116.501 1.00 14.33 ? 245  ALA D CA    1 
ATOM   9505  C  C     . ALA L  3 245 ? 89.380  54.559  115.340 1.00 15.54 ? 245  ALA D C     1 
ATOM   9506  O  O     . ALA L  3 245 ? 89.449  53.598  114.567 1.00 14.21 ? 245  ALA D O     1 
ATOM   9507  C  CB    . ALA L  3 245 ? 91.434  53.582  116.469 1.00 15.05 ? 245  ALA D CB    1 
ATOM   9508  N  N     . LEU L  3 246 ? 88.456  55.506  115.212 1.00 13.20 ? 246  LEU D N     1 
ATOM   9509  C  CA    . LEU L  3 246 ? 87.412  55.375  114.203 1.00 13.24 ? 246  LEU D CA    1 
ATOM   9510  C  C     . LEU L  3 246 ? 87.893  55.360  112.756 1.00 14.56 ? 246  LEU D C     1 
ATOM   9511  O  O     . LEU L  3 246 ? 87.394  54.559  111.953 1.00 14.14 ? 246  LEU D O     1 
ATOM   9512  C  CB    . LEU L  3 246 ? 86.365  56.493  114.364 1.00 13.86 ? 246  LEU D CB    1 
ATOM   9513  C  CG    . LEU L  3 246 ? 85.063  56.227  113.590 1.00 13.35 ? 246  LEU D CG    1 
ATOM   9514  C  CD1   . LEU L  3 246 ? 84.128  55.335  114.421 1.00 14.18 ? 246  LEU D CD1   1 
ATOM   9515  C  CD2   . LEU L  3 246 ? 84.360  57.572  113.288 1.00 14.34 ? 246  LEU D CD2   1 
ATOM   9516  N  N     . TYR L  3 247 ? 88.851  56.230  112.424 1.00 15.98 ? 247  TYR D N     1 
ATOM   9517  C  CA    . TYR L  3 247 ? 89.296  56.298  111.018 1.00 14.64 ? 247  TYR D CA    1 
ATOM   9518  C  C     . TYR L  3 247 ? 89.972  55.007  110.608 1.00 17.12 ? 247  TYR D C     1 
ATOM   9519  O  O     . TYR L  3 247 ? 89.794  54.529  109.471 1.00 18.21 ? 247  TYR D O     1 
ATOM   9520  C  CB    . TYR L  3 247 ? 90.263  57.458  110.820 1.00 16.41 ? 247  TYR D CB    1 
ATOM   9521  C  CG    . TYR L  3 247 ? 89.790  58.738  111.482 1.00 14.01 ? 247  TYR D CG    1 
ATOM   9522  C  CD1   . TYR L  3 247 ? 90.687  59.526  112.196 1.00 14.83 ? 247  TYR D CD1   1 
ATOM   9523  C  CD2   . TYR L  3 247 ? 88.468  59.148  111.393 1.00 16.11 ? 247  TYR D CD2   1 
ATOM   9524  C  CE1   . TYR L  3 247 ? 90.274  60.703  112.815 1.00 15.63 ? 247  TYR D CE1   1 
ATOM   9525  C  CE2   . TYR L  3 247 ? 88.040  60.337  112.012 1.00 15.14 ? 247  TYR D CE2   1 
ATOM   9526  C  CZ    . TYR L  3 247 ? 88.954  61.093  112.715 1.00 13.21 ? 247  TYR D CZ    1 
ATOM   9527  O  OH    . TYR L  3 247 ? 88.574  62.258  113.345 1.00 17.16 ? 247  TYR D OH    1 
ATOM   9528  N  N     . GLU L  3 248 ? 90.717  54.444  111.544 1.00 14.21 ? 248  GLU D N     1 
ATOM   9529  C  CA    . GLU L  3 248 ? 91.453  53.188  111.313 1.00 14.31 ? 248  GLU D CA    1 
ATOM   9530  C  C     . GLU L  3 248 ? 90.463  52.027  111.189 1.00 15.85 ? 248  GLU D C     1 
ATOM   9531  O  O     . GLU L  3 248 ? 90.633  51.133  110.353 1.00 15.82 ? 248  GLU D O     1 
ATOM   9532  C  CB    . GLU L  3 248 ? 92.446  52.928  112.461 1.00 15.85 ? 248  GLU D CB    1 
ATOM   9533  C  CG    . GLU L  3 248 ? 93.591  53.953  112.565 1.00 15.19 ? 248  GLU D CG    1 
ATOM   9534  C  CD    . GLU L  3 248 ? 93.196  55.277  113.223 1.00 18.77 ? 248  GLU D CD    1 
ATOM   9535  O  OE1   . GLU L  3 248 ? 92.036  55.409  113.671 1.00 17.39 ? 248  GLU D OE1   1 
ATOM   9536  O  OE2   . GLU L  3 248 ? 94.057  56.187  113.292 1.00 17.47 ? 248  GLU D OE2   1 
ATOM   9537  N  N     . LEU L  3 249 ? 89.438  52.019  112.050 1.00 15.06 ? 249  LEU D N     1 
ATOM   9538  C  CA    . LEU L  3 249 ? 88.410  50.999  111.991 1.00 14.04 ? 249  LEU D CA    1 
ATOM   9539  C  C     . LEU L  3 249 ? 87.747  51.017  110.602 1.00 15.87 ? 249  LEU D C     1 
ATOM   9540  O  O     . LEU L  3 249 ? 87.590  49.981  109.962 1.00 17.13 ? 249  LEU D O     1 
ATOM   9541  C  CB    . LEU L  3 249 ? 87.343  51.251  113.085 1.00 14.42 ? 249  LEU D CB    1 
ATOM   9542  C  CG    . LEU L  3 249 ? 86.072  50.385  113.046 1.00 13.94 ? 249  LEU D CG    1 
ATOM   9543  C  CD1   . LEU L  3 249 ? 86.429  48.881  113.121 1.00 16.76 ? 249  LEU D CD1   1 
ATOM   9544  C  CD2   . LEU L  3 249 ? 85.155  50.772  114.234 1.00 14.78 ? 249  LEU D CD2   1 
ATOM   9545  N  N     . GLU L  3 250 ? 87.370  52.200  110.126 1.00 15.65 ? 250  GLU D N     1 
ATOM   9546  C  CA    . GLU L  3 250 ? 86.725  52.314  108.816 1.00 15.74 ? 250  GLU D CA    1 
ATOM   9547  C  C     . GLU L  3 250 ? 87.651  51.790  107.732 1.00 17.65 ? 250  GLU D C     1 
ATOM   9548  O  O     . GLU L  3 250 ? 87.230  51.015  106.858 1.00 19.40 ? 250  GLU D O     1 
ATOM   9549  C  CB    . GLU L  3 250 ? 86.372  53.782  108.515 1.00 19.02 ? 250  GLU D CB    1 
ATOM   9550  C  CG    . GLU L  3 250 ? 85.649  53.994  107.194 1.00 21.00 ? 250  GLU D CG    1 
ATOM   9551  C  CD    . GLU L  3 250 ? 85.408  55.485  106.895 1.00 29.64 ? 250  GLU D CD    1 
ATOM   9552  O  OE1   . GLU L  3 250 ? 86.116  56.342  107.476 1.00 30.42 ? 250  GLU D OE1   1 
ATOM   9553  O  OE2   . GLU L  3 250 ? 84.523  55.794  106.065 1.00 30.04 ? 250  GLU D OE2   1 
ATOM   9554  N  N     . GLN L  3 251 ? 88.901  52.205  107.785 1.00 18.13 ? 251  GLN D N     1 
ATOM   9555  C  CA    . GLN L  3 251 ? 89.853  51.771  106.759 1.00 19.20 ? 251  GLN D CA    1 
ATOM   9556  C  C     . GLN L  3 251 ? 90.042  50.257  106.712 1.00 19.97 ? 251  GLN D C     1 
ATOM   9557  O  O     . GLN L  3 251 ? 90.051  49.649  105.625 1.00 20.21 ? 251  GLN D O     1 
ATOM   9558  C  CB    . GLN L  3 251 ? 91.192  52.461  106.959 1.00 20.39 ? 251  GLN D CB    1 
ATOM   9559  C  CG    . GLN L  3 251 ? 92.129  52.248  105.762 1.00 31.37 ? 251  GLN D CG    1 
ATOM   9560  C  CD    . GLN L  3 251 ? 93.445  52.976  105.925 1.00 38.63 ? 251  GLN D CD    1 
ATOM   9561  O  OE1   . GLN L  3 251 ? 93.481  54.104  106.431 1.00 46.94 ? 251  GLN D OE1   1 
ATOM   9562  N  NE2   . GLN L  3 251 ? 94.539  52.343  105.494 1.00 39.94 ? 251  GLN D NE2   1 
ATOM   9563  N  N     . ILE L  3 252 ? 90.167  49.633  107.878 1.00 17.49 ? 252  ILE D N     1 
ATOM   9564  C  CA    . ILE L  3 252 ? 90.368  48.192  107.906 1.00 18.76 ? 252  ILE D CA    1 
ATOM   9565  C  C     . ILE L  3 252 ? 89.109  47.431  107.483 1.00 17.17 ? 252  ILE D C     1 
ATOM   9566  O  O     . ILE L  3 252 ? 89.201  46.402  106.823 1.00 17.89 ? 252  ILE D O     1 
ATOM   9567  C  CB    . ILE L  3 252 ? 90.891  47.714  109.302 1.00 20.19 ? 252  ILE D CB    1 
ATOM   9568  C  CG1   . ILE L  3 252 ? 91.318  46.246  109.215 1.00 23.01 ? 252  ILE D CG1   1 
ATOM   9569  C  CG2   . ILE L  3 252 ? 89.824  47.828  110.377 1.00 25.17 ? 252  ILE D CG2   1 
ATOM   9570  C  CD1   . ILE L  3 252 ? 92.390  45.957  108.132 1.00 27.29 ? 252  ILE D CD1   1 
ATOM   9571  N  N     . LEU L  3 253 ? 87.927  47.917  107.846 1.00 17.31 ? 253  LEU D N     1 
ATOM   9572  C  CA    . LEU L  3 253 ? 86.698  47.259  107.424 1.00 17.46 ? 253  LEU D CA    1 
ATOM   9573  C  C     . LEU L  3 253 ? 86.648  47.281  105.901 1.00 20.76 ? 253  LEU D C     1 
ATOM   9574  O  O     . LEU L  3 253 ? 86.214  46.310  105.276 1.00 21.92 ? 253  LEU D O     1 
ATOM   9575  C  CB    . LEU L  3 253 ? 85.473  47.977  107.991 1.00 17.84 ? 253  LEU D CB    1 
ATOM   9576  C  CG    . LEU L  3 253 ? 85.299  47.781  109.503 1.00 14.72 ? 253  LEU D CG    1 
ATOM   9577  C  CD1   . LEU L  3 253 ? 84.143  48.632  110.000 1.00 17.75 ? 253  LEU D CD1   1 
ATOM   9578  C  CD2   . LEU L  3 253 ? 85.056  46.299  109.805 1.00 17.94 ? 253  LEU D CD2   1 
ATOM   9579  N  N     . GLN L  3 254 ? 87.103  48.380  105.312 1.00 20.50 ? 254  GLN D N     1 
ATOM   9580  C  CA    . GLN L  3 254 ? 87.099  48.488  103.851 1.00 21.38 ? 254  GLN D CA    1 
ATOM   9581  C  C     . GLN L  3 254 ? 88.111  47.529  103.229 1.00 23.08 ? 254  GLN D C     1 
ATOM   9582  O  O     . GLN L  3 254 ? 87.793  46.821  102.270 1.00 24.59 ? 254  GLN D O     1 
ATOM   9583  C  CB    . GLN L  3 254 ? 87.433  49.912  103.432 1.00 25.42 ? 254  GLN D CB    1 
ATOM   9584  C  CG    . GLN L  3 254 ? 86.326  50.891  103.725 1.00 30.92 ? 254  GLN D CG    1 
ATOM   9585  C  CD    . GLN L  3 254 ? 86.742  52.311  103.443 1.00 43.51 ? 254  GLN D CD    1 
ATOM   9586  O  OE1   . GLN L  3 254 ? 87.885  52.705  103.714 1.00 47.63 ? 254  GLN D OE1   1 
ATOM   9587  N  NE2   . GLN L  3 254 ? 85.814  53.103  102.910 1.00 48.87 ? 254  GLN D NE2   1 
ATOM   9588  N  N     . SER L  3 255 ? 89.315  47.504  103.785 1.00 21.09 ? 255  SER D N     1 
ATOM   9589  C  CA    . SER L  3 255 ? 90.380  46.643  103.265 1.00 22.52 ? 255  SER D CA    1 
ATOM   9590  C  C     . SER L  3 255 ? 90.085  45.147  103.351 1.00 24.75 ? 255  SER D C     1 
ATOM   9591  O  O     . SER L  3 255 ? 90.488  44.372  102.467 1.00 24.94 ? 255  SER D O     1 
ATOM   9592  C  CB    . SER L  3 255 ? 91.705  46.940  103.974 1.00 23.94 ? 255  SER D CB    1 
ATOM   9593  O  OG    . SER L  3 255 ? 92.114  48.267  103.714 1.00 30.60 ? 255  SER D OG    1 
ATOM   9594  N  N     . LEU L  3 256 ? 89.385  44.743  104.407 1.00 21.51 ? 256  LEU D N     1 
ATOM   9595  C  CA    . LEU L  3 256 ? 89.033  43.336  104.643 1.00 19.85 ? 256  LEU D CA    1 
ATOM   9596  C  C     . LEU L  3 256 ? 87.776  42.928  103.898 1.00 22.58 ? 256  LEU D C     1 
ATOM   9597  O  O     . LEU L  3 256 ? 87.447  41.744  103.810 1.00 22.05 ? 256  LEU D O     1 
ATOM   9598  C  CB    . LEU L  3 256 ? 88.803  43.090  106.158 1.00 18.96 ? 256  LEU D CB    1 
ATOM   9599  C  CG    . LEU L  3 256 ? 90.018  43.130  107.084 1.00 24.48 ? 256  LEU D CG    1 
ATOM   9600  C  CD1   . LEU L  3 256 ? 89.551  43.230  108.550 1.00 21.64 ? 256  LEU D CD1   1 
ATOM   9601  C  CD2   . LEU L  3 256 ? 90.850  41.873  106.909 1.00 25.69 ? 256  LEU D CD2   1 
ATOM   9602  N  N     . ASN L  3 257 ? 87.070  43.916  103.365 1.00 23.77 ? 257  ASN D N     1 
ATOM   9603  C  CA    . ASN L  3 257 ? 85.824  43.667  102.685 1.00 25.23 ? 257  ASN D CA    1 
ATOM   9604  C  C     . ASN L  3 257 ? 84.787  42.947  103.535 1.00 25.01 ? 257  ASN D C     1 
ATOM   9605  O  O     . ASN L  3 257 ? 84.099  42.030  103.091 1.00 26.43 ? 257  ASN D O     1 
ATOM   9606  C  CB    . ASN L  3 257 ? 86.067  42.932  101.368 1.00 29.51 ? 257  ASN D CB    1 
ATOM   9607  C  CG    . ASN L  3 257 ? 86.254  43.895  100.224 1.00 38.53 ? 257  ASN D CG    1 
ATOM   9608  O  OD1   . ASN L  3 257 ? 87.359  44.371  99.969  1.00 43.09 ? 257  ASN D OD1   1 
ATOM   9609  N  ND2   . ASN L  3 257 ? 85.155  44.228  99.553  1.00 43.80 ? 257  ASN D ND2   1 
ATOM   9610  N  N     . TYR L  3 258 ? 84.683  43.377  104.790 1.00 21.26 ? 258  TYR D N     1 
ATOM   9611  C  CA    . TYR L  3 258 ? 83.694  42.828  105.690 1.00 20.68 ? 258  TYR D CA    1 
ATOM   9612  C  C     . TYR L  3 258 ? 82.496  43.743  105.441 1.00 24.33 ? 258  TYR D C     1 
ATOM   9613  O  O     . TYR L  3 258 ? 82.247  44.697  106.192 1.00 23.76 ? 258  TYR D O     1 
ATOM   9614  C  CB    . TYR L  3 258 ? 84.196  42.947  107.130 1.00 19.26 ? 258  TYR D CB    1 
ATOM   9615  C  CG    . TYR L  3 258 ? 85.269  41.938  107.500 1.00 20.42 ? 258  TYR D CG    1 
ATOM   9616  C  CD1   . TYR L  3 258 ? 85.930  42.017  108.730 1.00 16.23 ? 258  TYR D CD1   1 
ATOM   9617  C  CD2   . TYR L  3 258 ? 85.582  40.872  106.645 1.00 21.13 ? 258  TYR D CD2   1 
ATOM   9618  C  CE1   . TYR L  3 258 ? 86.855  41.074  109.110 1.00 17.37 ? 258  TYR D CE1   1 
ATOM   9619  C  CE2   . TYR L  3 258 ? 86.515  39.917  107.012 1.00 19.55 ? 258  TYR D CE2   1 
ATOM   9620  C  CZ    . TYR L  3 258 ? 87.144  40.015  108.243 1.00 19.17 ? 258  TYR D CZ    1 
ATOM   9621  O  OH    . TYR L  3 258 ? 88.029  39.049  108.652 1.00 20.37 ? 258  TYR D OH    1 
ATOM   9622  N  N     . GLU L  3 259 ? 81.751  43.445  104.380 1.00 25.42 ? 259  GLU D N     1 
ATOM   9623  C  CA    . GLU L  3 259 ? 80.618  44.277  103.985 1.00 27.28 ? 259  GLU D CA    1 
ATOM   9624  C  C     . GLU L  3 259 ? 79.512  44.509  105.003 1.00 23.60 ? 259  GLU D C     1 
ATOM   9625  O  O     . GLU L  3 259 ? 79.024  45.630  105.110 1.00 24.13 ? 259  GLU D O     1 
ATOM   9626  C  CB    . GLU L  3 259 ? 79.995  43.746  102.687 1.00 33.39 ? 259  GLU D CB    1 
ATOM   9627  C  CG    . GLU L  3 259 ? 80.947  43.724  101.496 1.00 45.64 ? 259  GLU D CG    1 
ATOM   9628  C  CD    . GLU L  3 259 ? 81.646  45.060  101.259 1.00 52.41 ? 259  GLU D CD    1 
ATOM   9629  O  OE1   . GLU L  3 259 ? 80.967  46.115  101.321 1.00 53.83 ? 259  GLU D OE1   1 
ATOM   9630  O  OE2   . GLU L  3 259 ? 82.877  45.052  100.999 1.00 54.28 ? 259  GLU D OE2   1 
ATOM   9631  N  N     . ASP L  3 260 ? 79.096  43.463  105.717 1.00 22.34 ? 260  ASP D N     1 
ATOM   9632  C  CA    . ASP L  3 260 ? 78.025  43.596  106.702 1.00 23.56 ? 260  ASP D CA    1 
ATOM   9633  C  C     . ASP L  3 260 ? 78.485  44.491  107.840 1.00 22.77 ? 260  ASP D C     1 
ATOM   9634  O  O     . ASP L  3 260 ? 77.731  45.333  108.311 1.00 22.60 ? 260  ASP D O     1 
ATOM   9635  C  CB    . ASP L  3 260 ? 77.612  42.253  107.305 1.00 29.86 ? 260  ASP D CB    1 
ATOM   9636  C  CG    . ASP L  3 260 ? 76.883  41.357  106.325 1.00 35.35 ? 260  ASP D CG    1 
ATOM   9637  O  OD1   . ASP L  3 260 ? 76.309  41.866  105.335 1.00 39.97 ? 260  ASP D OD1   1 
ATOM   9638  O  OD2   . ASP L  3 260 ? 76.872  40.132  106.568 1.00 39.31 ? 260  ASP D OD2   1 
ATOM   9639  N  N     . ALA L  3 261 ? 79.724  44.289  108.287 1.00 19.62 ? 261  ALA D N     1 
ATOM   9640  C  CA    . ALA L  3 261 ? 80.266  45.103  109.385 1.00 19.08 ? 261  ALA D CA    1 
ATOM   9641  C  C     . ALA L  3 261 ? 80.409  46.566  108.937 1.00 19.69 ? 261  ALA D C     1 
ATOM   9642  O  O     . ALA L  3 261 ? 80.148  47.485  109.718 1.00 17.33 ? 261  ALA D O     1 
ATOM   9643  C  CB    . ALA L  3 261 ? 81.630  44.529  109.840 1.00 19.57 ? 261  ALA D CB    1 
ATOM   9644  N  N     . LEU L  3 262 ? 80.818  46.784  107.684 1.00 17.64 ? 262  LEU D N     1 
ATOM   9645  C  CA    . LEU L  3 262 ? 80.965  48.145  107.148 1.00 19.54 ? 262  LEU D CA    1 
ATOM   9646  C  C     . LEU L  3 262 ? 79.581  48.796  107.090 1.00 21.87 ? 262  LEU D C     1 
ATOM   9647  O  O     . LEU L  3 262 ? 79.440  49.966  107.423 1.00 20.36 ? 262  LEU D O     1 
ATOM   9648  C  CB    . LEU L  3 262 ? 81.573  48.115  105.734 1.00 23.39 ? 262  LEU D CB    1 
ATOM   9649  C  CG    . LEU L  3 262 ? 82.750  49.031  105.368 1.00 28.13 ? 262  LEU D CG    1 
ATOM   9650  C  CD1   . LEU L  3 262 ? 82.601  49.393  103.892 1.00 31.15 ? 262  LEU D CD1   1 
ATOM   9651  C  CD2   . LEU L  3 262 ? 82.808  50.302  106.223 1.00 28.55 ? 262  LEU D CD2   1 
ATOM   9652  N  N     . ASP L  3 263 ? 78.564  48.034  106.679 1.00 20.72 ? 263  ASP D N     1 
ATOM   9653  C  CA    . ASP L  3 263 ? 77.203  48.569  106.607 1.00 20.29 ? 263  ASP D CA    1 
ATOM   9654  C  C     . ASP L  3 263 ? 76.746  49.029  107.996 1.00 18.57 ? 263  ASP D C     1 
ATOM   9655  O  O     . ASP L  3 263 ? 76.187  50.120  108.137 1.00 20.32 ? 263  ASP D O     1 
ATOM   9656  C  CB    . ASP L  3 263 ? 76.214  47.524  106.077 1.00 22.95 ? 263  ASP D CB    1 
ATOM   9657  C  CG    . ASP L  3 263 ? 76.346  47.298  104.577 1.00 26.49 ? 263  ASP D CG    1 
ATOM   9658  O  OD1   . ASP L  3 263 ? 77.092  48.050  103.916 1.00 32.20 ? 263  ASP D OD1   1 
ATOM   9659  O  OD2   . ASP L  3 263 ? 75.689  46.368  104.074 1.00 31.76 ? 263  ASP D OD2   1 
ATOM   9660  N  N     . LEU L  3 264 ? 76.983  48.198  109.009 1.00 17.06 ? 264  LEU D N     1 
ATOM   9661  C  CA    . LEU L  3 264 ? 76.580  48.533  110.384 1.00 16.62 ? 264  LEU D CA    1 
ATOM   9662  C  C     . LEU L  3 264 ? 77.373  49.748  110.887 1.00 17.66 ? 264  LEU D C     1 
ATOM   9663  O  O     . LEU L  3 264 ? 76.808  50.611  111.582 1.00 17.07 ? 264  LEU D O     1 
ATOM   9664  C  CB    . LEU L  3 264 ? 76.780  47.309  111.295 1.00 15.91 ? 264  LEU D CB    1 
ATOM   9665  C  CG    . LEU L  3 264 ? 76.427  47.482  112.788 1.00 15.56 ? 264  LEU D CG    1 
ATOM   9666  C  CD1   . LEU L  3 264 ? 74.974  47.965  112.958 1.00 16.83 ? 264  LEU D CD1   1 
ATOM   9667  C  CD2   . LEU L  3 264 ? 76.608  46.125  113.486 1.00 18.85 ? 264  LEU D CD2   1 
ATOM   9668  N  N     . PHE L  3 265 ? 78.675  49.782  110.599 1.00 17.53 ? 265  PHE D N     1 
ATOM   9669  C  CA    . PHE L  3 265 ? 79.536  50.915  110.935 1.00 17.12 ? 265  PHE D CA    1 
ATOM   9670  C  C     . PHE L  3 265 ? 78.873  52.192  110.384 1.00 18.92 ? 265  PHE D C     1 
ATOM   9671  O  O     . PHE L  3 265 ? 78.686  53.163  111.115 1.00 16.36 ? 265  PHE D O     1 
ATOM   9672  C  CB    . PHE L  3 265 ? 80.914  50.732  110.286 1.00 17.05 ? 265  PHE D CB    1 
ATOM   9673  C  CG    . PHE L  3 265 ? 81.828  51.916  110.415 1.00 15.70 ? 265  PHE D CG    1 
ATOM   9674  C  CD1   . PHE L  3 265 ? 82.679  52.053  111.517 1.00 18.10 ? 265  PHE D CD1   1 
ATOM   9675  C  CD2   . PHE L  3 265 ? 81.862  52.906  109.427 1.00 16.26 ? 265  PHE D CD2   1 
ATOM   9676  C  CE1   . PHE L  3 265 ? 83.554  53.158  111.625 1.00 16.05 ? 265  PHE D CE1   1 
ATOM   9677  C  CE2   . PHE L  3 265 ? 82.725  54.010  109.529 1.00 17.43 ? 265  PHE D CE2   1 
ATOM   9678  C  CZ    . PHE L  3 265 ? 83.574  54.139  110.628 1.00 18.79 ? 265  PHE D CZ    1 
ATOM   9679  N  N     . TYR L  3 266 ? 78.502  52.197  109.104 1.00 17.85 ? 266  TYR D N     1 
ATOM   9680  C  CA    . TYR L  3 266 ? 77.886  53.393  108.533 1.00 17.56 ? 266  TYR D CA    1 
ATOM   9681  C  C     . TYR L  3 266 ? 76.497  53.721  109.073 1.00 17.86 ? 266  TYR D C     1 
ATOM   9682  O  O     . TYR L  3 266 ? 76.128  54.899  109.152 1.00 17.89 ? 266  TYR D O     1 
ATOM   9683  C  CB    . TYR L  3 266 ? 77.880  53.322  106.991 1.00 20.76 ? 266  TYR D CB    1 
ATOM   9684  C  CG    . TYR L  3 266 ? 79.245  53.584  106.408 1.00 20.99 ? 266  TYR D CG    1 
ATOM   9685  C  CD1   . TYR L  3 266 ? 79.847  52.664  105.559 1.00 24.92 ? 266  TYR D CD1   1 
ATOM   9686  C  CD2   . TYR L  3 266 ? 79.958  54.743  106.733 1.00 23.84 ? 266  TYR D CD2   1 
ATOM   9687  C  CE1   . TYR L  3 266 ? 81.117  52.887  105.054 1.00 26.58 ? 266  TYR D CE1   1 
ATOM   9688  C  CE2   . TYR L  3 266 ? 81.237  54.974  106.235 1.00 27.94 ? 266  TYR D CE2   1 
ATOM   9689  C  CZ    . TYR L  3 266 ? 81.806  54.028  105.393 1.00 27.10 ? 266  TYR D CZ    1 
ATOM   9690  O  OH    . TYR L  3 266 ? 83.074  54.222  104.900 1.00 33.51 ? 266  TYR D OH    1 
ATOM   9691  N  N     . ILE L  3 267 ? 75.726  52.704  109.445 1.00 15.97 ? 267  ILE D N     1 
ATOM   9692  C  CA    . ILE L  3 267 ? 74.427  52.971  110.036 1.00 16.95 ? 267  ILE D CA    1 
ATOM   9693  C  C     . ILE L  3 267 ? 74.687  53.781  111.323 1.00 18.31 ? 267  ILE D C     1 
ATOM   9694  O  O     . ILE L  3 267 ? 73.996  54.763  111.607 1.00 17.84 ? 267  ILE D O     1 
ATOM   9695  C  CB    . ILE L  3 267 ? 73.729  51.670  110.427 1.00 18.55 ? 267  ILE D CB    1 
ATOM   9696  C  CG1   . ILE L  3 267 ? 73.164  51.019  109.164 1.00 23.36 ? 267  ILE D CG1   1 
ATOM   9697  C  CG2   . ILE L  3 267 ? 72.621  51.924  111.461 1.00 19.61 ? 267  ILE D CG2   1 
ATOM   9698  C  CD1   . ILE L  3 267 ? 72.638  49.632  109.408 1.00 22.75 ? 267  ILE D CD1   1 
ATOM   9699  N  N     . MET L  3 268 ? 75.667  53.345  112.104 1.00 17.37 ? 268  MET D N     1 
ATOM   9700  C  CA    . MET L  3 268 ? 75.965  54.030  113.377 1.00 14.27 ? 268  MET D CA    1 
ATOM   9701  C  C     . MET L  3 268 ? 76.575  55.401  113.191 1.00 15.70 ? 268  MET D C     1 
ATOM   9702  O  O     . MET L  3 268 ? 76.220  56.336  113.914 1.00 17.60 ? 268  MET D O     1 
ATOM   9703  C  CB    . MET L  3 268 ? 76.899  53.171  114.245 1.00 14.46 ? 268  MET D CB    1 
ATOM   9704  C  CG    . MET L  3 268 ? 76.233  51.899  114.769 1.00 16.05 ? 268  MET D CG    1 
ATOM   9705  S  SD    . MET L  3 268 ? 77.268  50.982  115.927 1.00 16.00 ? 268  MET D SD    1 
ATOM   9706  C  CE    . MET L  3 268 ? 78.570  50.344  114.786 1.00 16.48 ? 268  MET D CE    1 
ATOM   9707  N  N     . VAL L  3 269 ? 77.491  55.538  112.234 1.00 14.34 ? 269  VAL D N     1 
ATOM   9708  C  CA    . VAL L  3 269 ? 78.138  56.827  112.012 1.00 15.24 ? 269  VAL D CA    1 
ATOM   9709  C  C     . VAL L  3 269 ? 77.212  57.836  111.303 1.00 18.00 ? 269  VAL D C     1 
ATOM   9710  O  O     . VAL L  3 269 ? 77.031  58.970  111.761 1.00 17.68 ? 269  VAL D O     1 
ATOM   9711  C  CB    . VAL L  3 269 ? 79.459  56.648  111.219 1.00 17.16 ? 269  VAL D CB    1 
ATOM   9712  C  CG1   . VAL L  3 269 ? 80.009  58.006  110.816 1.00 15.73 ? 269  VAL D CG1   1 
ATOM   9713  C  CG2   . VAL L  3 269 ? 80.481  55.905  112.070 1.00 14.57 ? 269  VAL D CG2   1 
ATOM   9714  N  N     . ASN L  3 270 ? 76.607  57.424  110.196 1.00 19.03 ? 270  ASN D N     1 
ATOM   9715  C  CA    . ASN L  3 270 ? 75.680  58.308  109.509 1.00 21.13 ? 270  ASN D CA    1 
ATOM   9716  C  C     . ASN L  3 270 ? 74.461  58.587  110.381 1.00 20.47 ? 270  ASN D C     1 
ATOM   9717  O  O     . ASN L  3 270 ? 73.813  59.622  110.205 1.00 23.67 ? 270  ASN D O     1 
ATOM   9718  C  CB    . ASN L  3 270 ? 75.195  57.683  108.202 1.00 21.82 ? 270  ASN D CB    1 
ATOM   9719  C  CG    . ASN L  3 270 ? 76.301  57.533  107.183 1.00 25.83 ? 270  ASN D CG    1 
ATOM   9720  O  OD1   . ASN L  3 270 ? 77.313  58.226  107.231 1.00 30.46 ? 270  ASN D OD1   1 
ATOM   9721  N  ND2   . ASN L  3 270 ? 76.102  56.623  106.239 1.00 28.88 ? 270  ASN D ND2   1 
ATOM   9722  N  N     . GLY L  3 271 ? 74.151  57.664  111.299 1.00 17.59 ? 271  GLY D N     1 
ATOM   9723  C  CA    . GLY L  3 271 ? 73.024  57.785  112.212 1.00 18.60 ? 271  GLY D CA    1 
ATOM   9724  C  C     . GLY L  3 271 ? 73.352  58.537  113.503 1.00 16.51 ? 271  GLY D C     1 
ATOM   9725  O  O     . GLY L  3 271 ? 72.562  58.520  114.451 1.00 19.03 ? 271  GLY D O     1 
ATOM   9726  N  N     . LYS L  3 272 ? 74.525  59.160  113.543 1.00 16.26 ? 272  LYS D N     1 
ATOM   9727  C  CA    . LYS L  3 272 ? 74.930  59.975  114.697 1.00 16.77 ? 272  LYS D CA    1 
ATOM   9728  C  C     . LYS L  3 272 ? 74.911  59.227  116.035 1.00 18.56 ? 272  LYS D C     1 
ATOM   9729  O  O     . LYS L  3 272 ? 74.545  59.787  117.094 1.00 17.02 ? 272  LYS D O     1 
ATOM   9730  C  CB    . LYS L  3 272 ? 74.032  61.230  114.763 1.00 17.92 ? 272  LYS D CB    1 
ATOM   9731  C  CG    . LYS L  3 272 ? 73.882  61.949  113.409 1.00 25.59 ? 272  LYS D CG    1 
ATOM   9732  C  CD    . LYS L  3 272 ? 75.209  62.453  112.896 1.00 29.87 ? 272  LYS D CD    1 
ATOM   9733  C  CE    . LYS L  3 272 ? 75.065  63.209  111.559 1.00 39.88 ? 272  LYS D CE    1 
ATOM   9734  N  NZ    . LYS L  3 272 ? 74.636  62.319  110.435 1.00 43.05 ? 272  LYS D NZ    1 
ATOM   9735  N  N     . ARG L  3 273 ? 75.326  57.964  115.988 1.00 14.53 ? 273  ARG D N     1 
ATOM   9736  C  CA    . ARG L  3 273 ? 75.403  57.150  117.214 1.00 13.82 ? 273  ARG D CA    1 
ATOM   9737  C  C     . ARG L  3 273 ? 76.867  56.850  117.521 1.00 14.36 ? 273  ARG D C     1 
ATOM   9738  O  O     . ARG L  3 273 ? 77.204  56.403  118.617 1.00 12.65 ? 273  ARG D O     1 
ATOM   9739  C  CB    . ARG L  3 273 ? 74.676  55.799  117.044 1.00 14.09 ? 273  ARG D CB    1 
ATOM   9740  C  CG    . ARG L  3 273 ? 73.227  55.934  116.536 1.00 15.80 ? 273  ARG D CG    1 
ATOM   9741  C  CD    . ARG L  3 273 ? 72.428  57.010  117.325 1.00 15.39 ? 273  ARG D CD    1 
ATOM   9742  N  NE    . ARG L  3 273 ? 72.231  56.717  118.753 1.00 14.93 ? 273  ARG D NE    1 
ATOM   9743  C  CZ    . ARG L  3 273 ? 72.541  57.582  119.728 1.00 15.53 ? 273  ARG D CZ    1 
ATOM   9744  N  NH1   . ARG L  3 273 ? 73.074  58.758  119.425 1.00 15.34 ? 273  ARG D NH1   1 
ATOM   9745  N  NH2   . ARG L  3 273 ? 72.273  57.293  121.003 1.00 15.53 ? 273  ARG D NH2   1 
ATOM   9746  N  N     . LEU L  3 274 ? 77.744  57.083  116.555 1.00 12.50 ? 274  LEU D N     1 
ATOM   9747  C  CA    . LEU L  3 274 ? 79.155  56.750  116.738 1.00 12.94 ? 274  LEU D CA    1 
ATOM   9748  C  C     . LEU L  3 274 ? 80.070  57.778  116.071 1.00 15.29 ? 274  LEU D C     1 
ATOM   9749  O  O     . LEU L  3 274 ? 79.878  58.129  114.903 1.00 14.90 ? 274  LEU D O     1 
ATOM   9750  C  CB    . LEU L  3 274 ? 79.436  55.355  116.129 1.00 13.81 ? 274  LEU D CB    1 
ATOM   9751  C  CG    . LEU L  3 274 ? 80.853  54.782  116.283 1.00 13.27 ? 274  LEU D CG    1 
ATOM   9752  C  CD1   . LEU L  3 274 ? 81.161  54.475  117.762 1.00 13.79 ? 274  LEU D CD1   1 
ATOM   9753  C  CD2   . LEU L  3 274 ? 80.967  53.493  115.451 1.00 15.41 ? 274  LEU D CD2   1 
ATOM   9754  N  N     . LYS L  3 275 ? 81.070  58.233  116.818 1.00 13.40 ? 275  LYS D N     1 
ATOM   9755  C  CA    . LYS L  3 275 ? 82.035  59.228  116.337 1.00 12.46 ? 275  LYS D CA    1 
ATOM   9756  C  C     . LYS L  3 275 ? 83.449  58.808  116.766 1.00 10.84 ? 275  LYS D C     1 
ATOM   9757  O  O     . LYS L  3 275 ? 83.637  57.725  117.337 1.00 13.62 ? 275  LYS D O     1 
ATOM   9758  C  CB    . LYS L  3 275 ? 81.693  60.617  116.928 1.00 13.67 ? 275  LYS D CB    1 
ATOM   9759  C  CG    . LYS L  3 275 ? 80.316  61.142  116.531 1.00 12.42 ? 275  LYS D CG    1 
ATOM   9760  C  CD    . LYS L  3 275 ? 80.096  62.549  117.111 1.00 11.90 ? 275  LYS D CD    1 
ATOM   9761  C  CE    . LYS L  3 275 ? 78.721  63.080  116.787 1.00 12.82 ? 275  LYS D CE    1 
ATOM   9762  N  NZ    . LYS L  3 275 ? 78.631  64.541  117.174 1.00 15.43 ? 275  LYS D NZ    1 
ATOM   9763  N  N     . ASP L  3 276 ? 84.451  59.640  116.476 1.00 11.39 ? 276  ASP D N     1 
ATOM   9764  C  CA    . ASP L  3 276 ? 85.829  59.337  116.857 1.00 12.14 ? 276  ASP D CA    1 
ATOM   9765  C  C     . ASP L  3 276 ? 86.131  59.972  118.224 1.00 11.39 ? 276  ASP D C     1 
ATOM   9766  O  O     . ASP L  3 276 ? 85.484  60.942  118.621 1.00 13.85 ? 276  ASP D O     1 
ATOM   9767  C  CB    . ASP L  3 276 ? 86.801  59.946  115.827 1.00 12.71 ? 276  ASP D CB    1 
ATOM   9768  C  CG    . ASP L  3 276 ? 88.237  59.583  116.101 1.00 12.41 ? 276  ASP D CG    1 
ATOM   9769  O  OD1   . ASP L  3 276 ? 88.569  58.382  116.012 1.00 14.25 ? 276  ASP D OD1   1 
ATOM   9770  O  OD2   . ASP L  3 276 ? 89.055  60.478  116.421 1.00 13.11 ? 276  ASP D OD2   1 
ATOM   9771  N  N     . ILE L  3 277 ? 87.106  59.425  118.946 1.00 12.22 ? 277  ILE D N     1 
ATOM   9772  C  CA    . ILE L  3 277 ? 87.487  60.020  120.222 1.00 13.24 ? 277  ILE D CA    1 
ATOM   9773  C  C     . ILE L  3 277 ? 87.815  61.526  120.023 1.00 14.75 ? 277  ILE D C     1 
ATOM   9774  O  O     . ILE L  3 277 ? 87.539  62.344  120.920 1.00 14.74 ? 277  ILE D O     1 
ATOM   9775  C  CB    . ILE L  3 277 ? 88.712  59.254  120.810 1.00 16.93 ? 277  ILE D CB    1 
ATOM   9776  C  CG1   . ILE L  3 277 ? 89.148  59.836  122.144 1.00 17.29 ? 277  ILE D CG1   1 
ATOM   9777  C  CG2   . ILE L  3 277 ? 89.852  59.285  119.831 1.00 17.18 ? 277  ILE D CG2   1 
ATOM   9778  C  CD1   . ILE L  3 277 ? 88.102  59.718  123.193 1.00 21.15 ? 277  ILE D CD1   1 
ATOM   9779  N  N     . SER L  3 278 ? 88.361  61.911  118.858 1.00 13.97 ? 278  SER D N     1 
ATOM   9780  C  CA    . SER L  3 278 ? 88.701  63.326  118.641 1.00 13.66 ? 278  SER D CA    1 
ATOM   9781  C  C     . SER L  3 278 ? 87.493  64.258  118.557 1.00 12.81 ? 278  SER D C     1 
ATOM   9782  O  O     . SER L  3 278 ? 87.643  65.484  118.671 1.00 14.68 ? 278  SER D O     1 
ATOM   9783  C  CB    . SER L  3 278 ? 89.568  63.499  117.374 1.00 13.46 ? 278  SER D CB    1 
ATOM   9784  O  OG    . SER L  3 278 ? 88.818  63.184  116.216 1.00 16.75 ? 278  SER D OG    1 
ATOM   9785  N  N     . ASP L  3 279 ? 86.298  63.698  118.387 1.00 13.01 ? 279  ASP D N     1 
ATOM   9786  C  CA    . ASP L  3 279 ? 85.079  64.504  118.341 1.00 13.21 ? 279  ASP D CA    1 
ATOM   9787  C  C     . ASP L  3 279 ? 84.581  64.828  119.735 1.00 13.45 ? 279  ASP D C     1 
ATOM   9788  O  O     . ASP L  3 279 ? 83.839  65.792  119.919 1.00 15.74 ? 279  ASP D O     1 
ATOM   9789  C  CB    . ASP L  3 279 ? 83.953  63.760  117.616 1.00 14.73 ? 279  ASP D CB    1 
ATOM   9790  C  CG    . ASP L  3 279 ? 84.245  63.559  116.153 1.00 14.96 ? 279  ASP D CG    1 
ATOM   9791  O  OD1   . ASP L  3 279 ? 84.394  64.573  115.456 1.00 15.36 ? 279  ASP D OD1   1 
ATOM   9792  O  OD2   . ASP L  3 279 ? 84.333  62.394  115.704 1.00 15.57 ? 279  ASP D OD2   1 
ATOM   9793  N  N     . LEU L  3 280 ? 84.965  64.013  120.720 1.00 12.09 ? 280  LEU D N     1 
ATOM   9794  C  CA    . LEU L  3 280 ? 84.448  64.224  122.075 1.00 15.02 ? 280  LEU D CA    1 
ATOM   9795  C  C     . LEU L  3 280 ? 84.706  65.589  122.742 1.00 11.96 ? 280  LEU D C     1 
ATOM   9796  O  O     . LEU L  3 280 ? 83.765  66.192  123.258 1.00 13.19 ? 280  LEU D O     1 
ATOM   9797  C  CB    . LEU L  3 280 ? 84.894  63.068  122.989 1.00 12.66 ? 280  LEU D CB    1 
ATOM   9798  C  CG    . LEU L  3 280 ? 84.417  63.180  124.456 1.00 13.02 ? 280  LEU D CG    1 
ATOM   9799  C  CD1   . LEU L  3 280 ? 82.904  63.270  124.540 1.00 15.98 ? 280  LEU D CD1   1 
ATOM   9800  C  CD2   . LEU L  3 280 ? 84.882  61.911  125.223 1.00 14.88 ? 280  LEU D CD2   1 
ATOM   9801  N  N     . PRO L  3 281 ? 85.961  66.091  122.736 1.00 12.96 ? 281  PRO D N     1 
ATOM   9802  C  CA    . PRO L  3 281 ? 86.213  67.402  123.376 1.00 15.34 ? 281  PRO D CA    1 
ATOM   9803  C  C     . PRO L  3 281 ? 85.293  68.511  122.811 1.00 14.35 ? 281  PRO D C     1 
ATOM   9804  O  O     . PRO L  3 281 ? 84.697  69.294  123.561 1.00 14.98 ? 281  PRO D O     1 
ATOM   9805  C  CB    . PRO L  3 281 ? 87.695  67.660  123.078 1.00 17.01 ? 281  PRO D CB    1 
ATOM   9806  C  CG    . PRO L  3 281 ? 88.285  66.232  123.001 1.00 17.61 ? 281  PRO D CG    1 
ATOM   9807  C  CD    . PRO L  3 281 ? 87.204  65.498  122.203 1.00 13.83 ? 281  PRO D CD    1 
ATOM   9808  N  N     . LEU L  3 282 ? 85.177  68.599  121.490 1.00 13.80 ? 282  LEU D N     1 
ATOM   9809  C  CA    . LEU L  3 282 ? 84.282  69.599  120.910 1.00 14.66 ? 282  LEU D CA    1 
ATOM   9810  C  C     . LEU L  3 282 ? 82.809  69.332  121.232 1.00 14.31 ? 282  LEU D C     1 
ATOM   9811  O  O     . LEU L  3 282 ? 82.044  70.272  121.437 1.00 14.24 ? 282  LEU D O     1 
ATOM   9812  C  CB    . LEU L  3 282 ? 84.477  69.689  119.368 1.00 16.98 ? 282  LEU D CB    1 
ATOM   9813  C  CG    . LEU L  3 282 ? 85.596  70.649  118.958 1.00 16.44 ? 282  LEU D CG    1 
ATOM   9814  C  CD1   . LEU L  3 282 ? 85.992  70.343  117.495 1.00 19.52 ? 282  LEU D CD1   1 
ATOM   9815  C  CD2   . LEU L  3 282 ? 85.127  72.117  119.111 1.00 18.75 ? 282  LEU D CD2   1 
ATOM   9816  N  N     . ASP L  3 283 ? 82.403  68.063  121.303 1.00 12.92 ? 283  ASP D N     1 
ATOM   9817  C  CA    . ASP L  3 283 ? 81.009  67.767  121.638 1.00 11.69 ? 283  ASP D CA    1 
ATOM   9818  C  C     . ASP L  3 283 ? 80.712  68.160  123.096 1.00 13.50 ? 283  ASP D C     1 
ATOM   9819  O  O     . ASP L  3 283 ? 79.553  68.425  123.433 1.00 16.14 ? 283  ASP D O     1 
ATOM   9820  C  CB    . ASP L  3 283 ? 80.683  66.293  121.392 1.00 13.49 ? 283  ASP D CB    1 
ATOM   9821  C  CG    . ASP L  3 283 ? 80.422  66.007  119.920 1.00 13.58 ? 283  ASP D CG    1 
ATOM   9822  O  OD1   . ASP L  3 283 ? 80.451  66.977  119.124 1.00 15.22 ? 283  ASP D OD1   1 
ATOM   9823  O  OD2   . ASP L  3 283 ? 80.167  64.840  119.564 1.00 15.58 ? 283  ASP D OD2   1 
ATOM   9824  N  N     . LEU L  3 284 ? 81.740  68.195  123.937 1.00 14.51 ? 284  LEU D N     1 
ATOM   9825  C  CA    . LEU L  3 284 ? 81.559  68.621  125.340 1.00 14.12 ? 284  LEU D CA    1 
ATOM   9826  C  C     . LEU L  3 284 ? 81.467  70.155  125.429 1.00 16.49 ? 284  LEU D C     1 
ATOM   9827  O  O     . LEU L  3 284 ? 81.242  70.718  126.508 1.00 16.63 ? 284  LEU D O     1 
ATOM   9828  C  CB    . LEU L  3 284 ? 82.733  68.149  126.199 1.00 15.54 ? 284  LEU D CB    1 
ATOM   9829  C  CG    . LEU L  3 284 ? 82.820  66.635  126.393 1.00 17.41 ? 284  LEU D CG    1 
ATOM   9830  C  CD1   . LEU L  3 284 ? 84.042  66.289  127.252 1.00 16.93 ? 284  LEU D CD1   1 
ATOM   9831  C  CD2   . LEU L  3 284 ? 81.553  66.159  127.107 1.00 18.46 ? 284  LEU D CD2   1 
ATOM   9832  N  N     . ALA L  3 285 ? 81.625  70.834  124.296 1.00 14.36 ? 285  ALA D N     1 
ATOM   9833  C  CA    . ALA L  3 285 ? 81.583  72.298  124.276 1.00 16.50 ? 285  ALA D CA    1 
ATOM   9834  C  C     . ALA L  3 285 ? 80.280  72.894  123.752 1.00 17.21 ? 285  ALA D C     1 
ATOM   9835  O  O     . ALA L  3 285 ? 80.160  74.112  123.640 1.00 18.44 ? 285  ALA D O     1 
ATOM   9836  C  CB    . ALA L  3 285 ? 82.786  72.847  123.447 1.00 16.88 ? 285  ALA D CB    1 
ATOM   9837  N  N     . VAL L  3 286 ? 79.287  72.059  123.452 1.00 17.30 ? 286  VAL D N     1 
ATOM   9838  C  CA    . VAL L  3 286 ? 78.028  72.592  122.905 1.00 20.85 ? 286  VAL D CA    1 
ATOM   9839  C  C     . VAL L  3 286 ? 77.303  73.473  123.933 1.00 23.30 ? 286  VAL D C     1 
ATOM   9840  O  O     . VAL L  3 286 ? 76.629  74.426  123.514 1.00 18.75 ? 286  VAL D O     1 
ATOM   9841  C  CB    . VAL L  3 286 ? 77.074  71.467  122.454 1.00 21.16 ? 286  VAL D CB    1 
ATOM   9842  C  CG1   . VAL L  3 286 ? 77.710  70.645  121.321 1.00 15.84 ? 286  VAL D CG1   1 
ATOM   9843  C  CG2   . VAL L  3 286 ? 76.750  70.588  123.633 1.00 21.15 ? 286  VAL D CG2   1 
ATOM   9844  O  OXT   . VAL L  3 286 ? 77.412  73.181  125.145 1.00 21.51 ? 286  VAL D OXT   1 
HETATM 9845  MG MG    . MG  M  4 .   ? 41.603  60.873  136.235 1.00 23.46 ? 2222 MG  I MG    1 
HETATM 9846  MG MG    . MG  N  4 .   ? 53.004  74.034  123.921 1.00 31.40 ? 4444 MG  J MG    1 
HETATM 9847  MG MG    . MG  O  4 .   ? 69.388  36.345  128.280 1.00 24.07 ? 6666 MG  K MG    1 
HETATM 9848  MG MG    . MG  P  4 .   ? 81.790  52.223  135.415 1.00 22.83 ? 8888 MG  L MG    1 
HETATM 9849  MG MG    . MG  Q  4 .   ? 52.469  76.172  126.865 1.00 15.90 ? 5555 MG  A MG    1 
HETATM 9850  C  C     . ACY R  5 .   ? 53.676  73.302  127.028 1.00 26.03 ? 2001 ACY A C     1 
HETATM 9851  O  O     . ACY R  5 .   ? 53.257  74.244  127.856 1.00 23.67 ? 2001 ACY A O     1 
HETATM 9852  O  OXT   . ACY R  5 .   ? 53.726  73.377  125.791 1.00 25.39 ? 2001 ACY A OXT   1 
HETATM 9853  C  CH3   . ACY R  5 .   ? 54.155  72.016  127.682 1.00 21.69 ? 2001 ACY A CH3   1 
HETATM 9854  MG MG    . MG  S  4 .   ? 39.778  60.870  133.115 1.00 15.26 ? 3333 MG  B MG    1 
HETATM 9855  C  C     . ACY T  5 .   ? 42.753  60.226  133.208 1.00 22.42 ? 3002 ACY B C     1 
HETATM 9856  O  O     . ACY T  5 .   ? 42.575  60.126  134.471 1.00 23.68 ? 3002 ACY B O     1 
HETATM 9857  O  OXT   . ACY T  5 .   ? 41.851  60.354  132.318 1.00 21.62 ? 3002 ACY B OXT   1 
HETATM 9858  C  CH3   . ACY T  5 .   ? 44.202  60.177  132.832 1.00 20.03 ? 3002 ACY B CH3   1 
HETATM 9859  MG MG    . MG  U  4 .   ? 70.314  35.071  131.610 1.00 13.93 ? 7777 MG  C MG    1 
HETATM 9860  C  C     . ACY V  5 .   ? 69.074  37.953  131.118 1.00 22.31 ? 4003 ACY C C     1 
HETATM 9861  O  O     . ACY V  5 .   ? 69.601  37.246  132.098 1.00 17.79 ? 4003 ACY C O     1 
HETATM 9862  O  OXT   . ACY V  5 .   ? 68.732  37.512  130.009 1.00 21.12 ? 4003 ACY C OXT   1 
HETATM 9863  C  CH3   . ACY V  5 .   ? 68.854  39.419  131.406 1.00 19.91 ? 4003 ACY C CH3   1 
HETATM 9864  MG MG    . MG  W  4 .   ? 83.439  51.389  132.335 1.00 11.96 ? 9999 MG  D MG    1 
HETATM 9865  C  C     . ACY X  5 .   ? 80.422  52.050  132.479 1.00 23.31 ? 5004 ACY D C     1 
HETATM 9866  O  O     . ACY X  5 .   ? 80.749  52.613  133.571 1.00 21.66 ? 5004 ACY D O     1 
HETATM 9867  O  OXT   . ACY X  5 .   ? 81.229  51.562  131.621 1.00 18.75 ? 5004 ACY D OXT   1 
HETATM 9868  C  CH3   . ACY X  5 .   ? 78.915  52.008  132.260 1.00 19.55 ? 5004 ACY D CH3   1 
HETATM 9869  O  O     . HOH Y  6 .   ? 37.198  67.405  139.182 1.00 37.62 ? 58   HOH E O     1 
HETATM 9870  O  O     . HOH Y  6 .   ? 37.959  64.671  138.916 1.00 30.75 ? 261  HOH E O     1 
HETATM 9871  O  O     . HOH Y  6 .   ? 34.975  67.777  137.943 1.00 22.41 ? 284  HOH E O     1 
HETATM 9872  O  O     . HOH Y  6 .   ? 44.254  72.337  139.069 1.00 18.30 ? 385  HOH E O     1 
HETATM 9873  O  O     . HOH Y  6 .   ? 32.777  76.992  144.776 1.00 24.79 ? 434  HOH E O     1 
HETATM 9874  O  O     . HOH Y  6 .   ? 32.380  77.403  146.926 1.00 38.49 ? 436  HOH E O     1 
HETATM 9875  O  O     . HOH Y  6 .   ? 31.931  74.977  145.231 1.00 37.32 ? 438  HOH E O     1 
HETATM 9876  O  O     . HOH Y  6 .   ? 34.971  76.319  145.192 1.00 42.46 ? 439  HOH E O     1 
HETATM 9877  O  O     . HOH Y  6 .   ? 37.951  76.374  145.708 1.00 38.65 ? 440  HOH E O     1 
HETATM 9878  O  O     . HOH Y  6 .   ? 45.489  71.354  141.281 1.00 24.61 ? 453  HOH E O     1 
HETATM 9879  O  O     . HOH Y  6 .   ? 45.555  70.713  145.841 1.00 40.20 ? 455  HOH E O     1 
HETATM 9880  O  O     . HOH Y  6 .   ? 38.386  78.456  148.690 1.00 36.61 ? 570  HOH E O     1 
HETATM 9881  O  O     . HOH Y  6 .   ? 42.944  74.179  144.021 1.00 39.43 ? 625  HOH E O     1 
HETATM 9882  O  O     . HOH Y  6 .   ? 47.804  67.783  141.745 1.00 37.63 ? 630  HOH E O     1 
HETATM 9883  O  O     . HOH Y  6 .   ? 30.728  77.961  144.531 1.00 32.51 ? 1100 HOH E O     1 
HETATM 9884  O  O     . HOH Z  6 .   ? 46.776  88.411  120.198 1.00 32.31 ? 18   HOH I O     1 
HETATM 9885  O  O     . HOH Z  6 .   ? 35.267  76.675  127.854 1.00 19.75 ? 42   HOH I O     1 
HETATM 9886  O  O     . HOH Z  6 .   ? 33.833  71.725  131.377 1.00 19.03 ? 54   HOH I O     1 
HETATM 9887  O  O     . HOH Z  6 .   ? 35.460  60.705  132.052 1.00 17.51 ? 56   HOH I O     1 
HETATM 9888  O  O     . HOH Z  6 .   ? 39.964  62.635  131.829 1.00 18.27 ? 57   HOH I O     1 
HETATM 9889  O  O     . HOH Z  6 .   ? 33.454  78.259  119.701 1.00 34.65 ? 143  HOH I O     1 
HETATM 9890  O  O     . HOH Z  6 .   ? 45.107  80.689  119.408 1.00 37.15 ? 145  HOH I O     1 
HETATM 9891  O  O     . HOH Z  6 .   ? 36.974  84.006  123.829 1.00 28.49 ? 200  HOH I O     1 
HETATM 9892  O  O     . HOH Z  6 .   ? 37.395  79.456  125.698 1.00 21.47 ? 222  HOH I O     1 
HETATM 9893  O  O     . HOH Z  6 .   ? 29.038  77.764  124.145 1.00 53.41 ? 230  HOH I O     1 
HETATM 9894  O  O     . HOH Z  6 .   ? 43.396  62.136  136.462 1.00 34.73 ? 259  HOH I O     1 
HETATM 9895  O  O     . HOH Z  6 .   ? 40.451  65.324  129.714 1.00 21.94 ? 266  HOH I O     1 
HETATM 9896  O  O     . HOH Z  6 .   ? 41.213  66.245  131.972 1.00 21.36 ? 298  HOH I O     1 
HETATM 9897  O  O     . HOH Z  6 .   ? 44.386  65.066  136.255 1.00 30.26 ? 360  HOH I O     1 
HETATM 9898  O  O     . HOH Z  6 .   ? 34.981  79.683  126.793 1.00 25.82 ? 390  HOH I O     1 
HETATM 9899  O  O     . HOH Z  6 .   ? 47.935  87.827  117.841 1.00 40.57 ? 404  HOH I O     1 
HETATM 9900  O  O     . HOH Z  6 .   ? 35.339  78.676  128.774 1.00 27.85 ? 411  HOH I O     1 
HETATM 9901  O  O     . HOH Z  6 .   ? 34.029  74.782  129.586 1.00 24.27 ? 414  HOH I O     1 
HETATM 9902  O  O     . HOH Z  6 .   ? 28.306  73.897  127.391 1.00 32.26 ? 419  HOH I O     1 
HETATM 9903  O  O     . HOH Z  6 .   ? 31.242  81.585  119.442 1.00 53.79 ? 443  HOH I O     1 
HETATM 9904  O  O     . HOH Z  6 .   ? 29.807  77.605  121.503 1.00 48.32 ? 444  HOH I O     1 
HETATM 9905  O  O     . HOH Z  6 .   ? 30.337  72.924  120.925 1.00 34.36 ? 445  HOH I O     1 
HETATM 9906  O  O     . HOH Z  6 .   ? 33.104  71.453  122.244 1.00 32.55 ? 446  HOH I O     1 
HETATM 9907  O  O     . HOH Z  6 .   ? 27.138  74.102  123.728 1.00 33.38 ? 675  HOH I O     1 
HETATM 9908  O  O     . HOH Z  6 .   ? 34.445  68.983  122.973 1.00 27.48 ? 676  HOH I O     1 
HETATM 9909  O  O     . HOH Z  6 .   ? 35.919  78.388  115.697 1.00 41.56 ? 677  HOH I O     1 
HETATM 9910  O  O     . HOH Z  6 .   ? 33.835  79.185  117.279 1.00 39.58 ? 933  HOH I O     1 
HETATM 9911  O  O     . HOH Z  6 .   ? 33.203  81.686  126.143 1.00 32.54 ? 934  HOH I O     1 
HETATM 9912  O  O     . HOH Z  6 .   ? 34.523  83.782  127.142 1.00 49.74 ? 935  HOH I O     1 
HETATM 9913  O  O     . HOH Z  6 .   ? 36.293  82.079  116.306 1.00 39.39 ? 937  HOH I O     1 
HETATM 9914  O  O     . HOH Z  6 .   ? 37.778  85.591  116.674 1.00 49.48 ? 938  HOH I O     1 
HETATM 9915  O  O     . HOH Z  6 .   ? 42.490  89.631  119.411 1.00 54.92 ? 939  HOH I O     1 
HETATM 9916  O  O     . HOH Z  6 .   ? 33.481  78.048  114.259 1.00 51.29 ? 1002 HOH I O     1 
HETATM 9917  O  O     . HOH Z  6 .   ? 39.241  88.036  120.136 1.00 46.35 ? 1105 HOH I O     1 
HETATM 9918  O  O     . HOH Z  6 .   ? 29.708  67.617  126.235 1.00 60.00 ? 1242 HOH I O     1 
HETATM 9919  O  O     . HOH Z  6 .   ? 37.353  80.005  115.746 1.00 53.28 ? 1279 HOH I O     1 
HETATM 9920  O  O     . HOH AA 6 .   ? 52.296  74.585  121.918 1.00 26.04 ? 22   HOH F O     1 
HETATM 9921  O  O     . HOH AA 6 .   ? 49.025  76.801  120.640 1.00 31.44 ? 45   HOH F O     1 
HETATM 9922  O  O     . HOH AA 6 .   ? 45.495  75.197  117.675 1.00 34.11 ? 116  HOH F O     1 
HETATM 9923  O  O     . HOH AA 6 .   ? 45.221  78.903  121.363 1.00 27.03 ? 406  HOH F O     1 
HETATM 9924  O  O     . HOH AA 6 .   ? 42.964  68.982  120.489 1.00 18.62 ? 765  HOH F O     1 
HETATM 9925  O  O     . HOH AA 6 .   ? 44.237  67.917  118.452 1.00 26.67 ? 766  HOH F O     1 
HETATM 9926  O  O     . HOH AA 6 .   ? 49.739  69.520  118.880 1.00 45.36 ? 767  HOH F O     1 
HETATM 9927  O  O     . HOH AA 6 .   ? 46.338  76.843  120.514 1.00 31.92 ? 1064 HOH F O     1 
HETATM 9928  O  O     . HOH AA 6 .   ? 36.496  76.799  113.887 1.00 56.21 ? 1080 HOH F O     1 
HETATM 9929  O  O     . HOH AA 6 .   ? 36.410  79.607  113.515 1.00 45.49 ? 1097 HOH F O     1 
HETATM 9930  O  O     . HOH AA 6 .   ? 36.312  70.343  110.312 1.00 47.61 ? 1277 HOH F O     1 
HETATM 9931  O  O     . HOH AA 6 .   ? 35.164  74.338  111.361 1.00 55.57 ? 1278 HOH F O     1 
HETATM 9932  O  O     . HOH BA 6 .   ? 51.594  80.497  127.564 1.00 15.94 ? 43   HOH J O     1 
HETATM 9933  O  O     . HOH BA 6 .   ? 50.696  75.685  127.996 1.00 18.19 ? 221  HOH J O     1 
HETATM 9934  O  O     . HOH BA 6 .   ? 47.908  74.719  129.856 1.00 26.43 ? 236  HOH J O     1 
HETATM 9935  O  O     . HOH BA 6 .   ? 26.000  64.202  138.134 1.00 32.54 ? 253  HOH J O     1 
HETATM 9936  O  O     . HOH BA 6 .   ? 33.874  76.944  129.628 1.00 22.87 ? 268  HOH J O     1 
HETATM 9937  O  O     . HOH BA 6 .   ? 29.220  61.248  141.945 1.00 48.62 ? 282  HOH J O     1 
HETATM 9938  O  O     . HOH BA 6 .   ? 28.505  74.523  134.253 1.00 25.75 ? 332  HOH J O     1 
HETATM 9939  O  O     . HOH BA 6 .   ? 37.431  78.814  128.827 1.00 21.02 ? 389  HOH J O     1 
HETATM 9940  O  O     . HOH BA 6 .   ? 36.939  84.894  130.833 1.00 35.83 ? 393  HOH J O     1 
HETATM 9941  O  O     . HOH BA 6 .   ? 35.927  86.536  132.986 1.00 53.70 ? 396  HOH J O     1 
HETATM 9942  O  O     . HOH BA 6 .   ? 36.621  85.823  135.344 1.00 53.37 ? 400  HOH J O     1 
HETATM 9943  O  O     . HOH BA 6 .   ? 40.523  79.678  127.347 1.00 21.84 ? 407  HOH J O     1 
HETATM 9944  O  O     . HOH BA 6 .   ? 35.735  77.425  130.621 1.00 20.49 ? 412  HOH J O     1 
HETATM 9945  O  O     . HOH BA 6 .   ? 33.215  74.934  132.694 1.00 20.53 ? 415  HOH J O     1 
HETATM 9946  O  O     . HOH BA 6 .   ? 32.548  77.341  131.417 1.00 24.50 ? 416  HOH J O     1 
HETATM 9947  O  O     . HOH BA 6 .   ? 31.903  76.740  128.348 1.00 44.81 ? 417  HOH J O     1 
HETATM 9948  O  O     . HOH BA 6 .   ? 30.094  75.159  129.282 1.00 39.59 ? 418  HOH J O     1 
HETATM 9949  O  O     . HOH BA 6 .   ? 30.763  78.852  127.593 1.00 41.04 ? 421  HOH J O     1 
HETATM 9950  O  O     . HOH BA 6 .   ? 30.324  78.524  131.934 1.00 34.37 ? 422  HOH J O     1 
HETATM 9951  O  O     . HOH BA 6 .   ? 40.400  80.655  136.407 1.00 28.37 ? 425  HOH J O     1 
HETATM 9952  O  O     . HOH BA 6 .   ? 42.980  80.177  136.119 1.00 22.22 ? 427  HOH J O     1 
HETATM 9953  O  O     . HOH BA 6 .   ? 33.116  79.479  138.644 1.00 27.00 ? 429  HOH J O     1 
HETATM 9954  O  O     . HOH BA 6 .   ? 32.390  78.810  141.073 1.00 31.26 ? 430  HOH J O     1 
HETATM 9955  O  O     . HOH BA 6 .   ? 33.752  83.093  136.553 1.00 51.51 ? 431  HOH J O     1 
HETATM 9956  O  O     . HOH BA 6 .   ? 29.183  81.970  133.642 1.00 55.21 ? 433  HOH J O     1 
HETATM 9957  O  O     . HOH BA 6 .   ? 32.907  76.739  142.600 1.00 32.28 ? 435  HOH J O     1 
HETATM 9958  O  O     . HOH BA 6 .   ? 49.557  70.820  123.990 1.00 36.22 ? 450  HOH J O     1 
HETATM 9959  O  O     . HOH BA 6 .   ? 33.012  67.913  139.831 1.00 26.18 ? 457  HOH J O     1 
HETATM 9960  O  O     . HOH BA 6 .   ? 26.771  72.991  141.201 1.00 37.09 ? 632  HOH J O     1 
HETATM 9961  O  O     . HOH BA 6 .   ? 27.494  78.590  134.449 1.00 53.20 ? 942  HOH J O     1 
HETATM 9962  O  O     . HOH BA 6 .   ? 29.411  76.225  141.140 1.00 50.86 ? 943  HOH J O     1 
HETATM 9963  O  O     . HOH BA 6 .   ? 27.028  77.647  136.650 1.00 46.53 ? 944  HOH J O     1 
HETATM 9964  O  O     . HOH BA 6 .   ? 25.527  76.377  139.382 1.00 47.42 ? 945  HOH J O     1 
HETATM 9965  O  O     . HOH BA 6 .   ? 27.685  72.784  143.817 1.00 39.14 ? 946  HOH J O     1 
HETATM 9966  O  O     . HOH BA 6 .   ? 33.754  84.096  134.338 1.00 42.51 ? 1216 HOH J O     1 
HETATM 9967  O  O     . HOH CA 6 .   ? 84.159  36.311  113.416 1.00 31.51 ? 5    HOH G O     1 
HETATM 9968  O  O     . HOH CA 6 .   ? 79.201  40.222  122.687 1.00 14.64 ? 6    HOH G O     1 
HETATM 9969  O  O     . HOH CA 6 .   ? 76.402  33.643  117.666 1.00 39.11 ? 7    HOH G O     1 
HETATM 9970  O  O     . HOH CA 6 .   ? 70.647  41.549  119.658 1.00 47.22 ? 8    HOH G O     1 
HETATM 9971  O  O     . HOH CA 6 .   ? 73.643  42.623  120.520 1.00 31.70 ? 9    HOH G O     1 
HETATM 9972  O  O     . HOH CA 6 .   ? 77.825  40.673  120.491 1.00 21.52 ? 10   HOH G O     1 
HETATM 9973  O  O     . HOH CA 6 .   ? 81.827  40.441  117.533 1.00 32.10 ? 11   HOH G O     1 
HETATM 9974  O  O     . HOH CA 6 .   ? 75.741  32.728  125.031 1.00 28.50 ? 12   HOH G O     1 
HETATM 9975  O  O     . HOH CA 6 .   ? 73.115  32.730  125.566 1.00 36.51 ? 13   HOH G O     1 
HETATM 9976  O  O     . HOH CA 6 .   ? 74.612  32.509  122.608 1.00 45.67 ? 14   HOH G O     1 
HETATM 9977  O  O     . HOH CA 6 .   ? 78.272  39.885  113.243 1.00 52.37 ? 15   HOH G O     1 
HETATM 9978  O  O     . HOH CA 6 .   ? 77.302  31.422  114.654 1.00 43.73 ? 16   HOH G O     1 
HETATM 9979  O  O     . HOH CA 6 .   ? 81.870  30.986  106.101 1.00 43.38 ? 17   HOH G O     1 
HETATM 9980  O  O     . HOH CA 6 .   ? 72.988  44.560  119.158 1.00 52.21 ? 18   HOH G O     1 
HETATM 9981  O  O     . HOH DA 6 .   ? 71.262  31.127  133.391 1.00 13.94 ? 67   HOH K O     1 
HETATM 9982  O  O     . HOH DA 6 .   ? 72.772  39.558  126.923 1.00 31.34 ? 238  HOH K O     1 
HETATM 9983  O  O     . HOH DA 6 .   ? 70.217  38.212  127.495 1.00 34.00 ? 271  HOH K O     1 
HETATM 9984  O  O     . HOH DA 6 .   ? 75.382  37.720  131.214 1.00 17.95 ? 281  HOH K O     1 
HETATM 9985  O  O     . HOH DA 6 .   ? 86.759  28.952  133.598 1.00 40.05 ? 295  HOH K O     1 
HETATM 9986  O  O     . HOH DA 6 .   ? 85.600  32.709  132.759 1.00 19.37 ? 300  HOH K O     1 
HETATM 9987  O  O     . HOH DA 6 .   ? 90.054  37.545  135.167 1.00 18.92 ? 304  HOH K O     1 
HETATM 9988  O  O     . HOH DA 6 .   ? 74.961  37.213  133.744 1.00 21.14 ? 313  HOH K O     1 
HETATM 9989  O  O     . HOH DA 6 .   ? 72.258  35.840  132.339 1.00 16.07 ? 328  HOH K O     1 
HETATM 9990  O  O     . HOH DA 6 .   ? 87.443  34.640  134.069 1.00 17.38 ? 329  HOH K O     1 
HETATM 9991  O  O     . HOH DA 6 .   ? 82.324  31.639  131.834 1.00 17.57 ? 346  HOH K O     1 
HETATM 9992  O  O     . HOH DA 6 .   ? 97.361  49.356  137.033 1.00 26.82 ? 365  HOH K O     1 
HETATM 9993  O  O     . HOH DA 6 .   ? 80.888  33.454  140.322 1.00 22.71 ? 378  HOH K O     1 
HETATM 9994  O  O     . HOH DA 6 .   ? 89.709  32.791  132.831 1.00 27.45 ? 459  HOH K O     1 
HETATM 9995  O  O     . HOH DA 6 .   ? 90.663  35.015  134.480 1.00 22.52 ? 461  HOH K O     1 
HETATM 9996  O  O     . HOH DA 6 .   ? 92.977  33.938  135.006 1.00 35.25 ? 462  HOH K O     1 
HETATM 9997  O  O     . HOH DA 6 .   ? 94.936  38.177  136.008 1.00 23.30 ? 463  HOH K O     1 
HETATM 9998  O  O     . HOH DA 6 .   ? 92.241  32.523  130.846 1.00 37.16 ? 465  HOH K O     1 
HETATM 9999  O  O     . HOH DA 6 .   ? 86.472  27.695  136.178 1.00 31.79 ? 472  HOH K O     1 
HETATM 10000 O  O     . HOH DA 6 .   ? 86.934  27.336  139.725 1.00 36.44 ? 473  HOH K O     1 
HETATM 10001 O  O     . HOH DA 6 .   ? 86.086  30.680  142.436 1.00 29.65 ? 475  HOH K O     1 
HETATM 10002 O  O     . HOH DA 6 .   ? 90.462  30.753  140.710 1.00 43.75 ? 482  HOH K O     1 
HETATM 10003 O  O     . HOH DA 6 .   ? 90.812  34.669  141.949 1.00 25.70 ? 485  HOH K O     1 
HETATM 10004 O  O     . HOH DA 6 .   ? 83.574  32.917  140.701 1.00 28.74 ? 562  HOH K O     1 
HETATM 10005 O  O     . HOH DA 6 .   ? 89.895  29.239  138.627 1.00 48.79 ? 563  HOH K O     1 
HETATM 10006 O  O     . HOH DA 6 .   ? 92.202  35.793  143.913 1.00 38.11 ? 813  HOH K O     1 
HETATM 10007 O  O     . HOH DA 6 .   ? 94.857  34.478  141.819 1.00 56.83 ? 814  HOH K O     1 
HETATM 10008 O  O     . HOH DA 6 .   ? 91.606  38.184  144.850 1.00 33.43 ? 815  HOH K O     1 
HETATM 10009 O  O     . HOH DA 6 .   ? 94.261  39.436  144.530 1.00 48.48 ? 816  HOH K O     1 
HETATM 10010 O  O     . HOH DA 6 .   ? 87.853  31.172  133.940 1.00 32.51 ? 828  HOH K O     1 
HETATM 10011 O  O     . HOH DA 6 .   ? 90.538  30.617  134.611 1.00 39.97 ? 1098 HOH K O     1 
HETATM 10012 O  O     . HOH DA 6 .   ? 96.989  35.772  138.680 1.00 57.36 ? 1192 HOH K O     1 
HETATM 10013 O  O     . HOH EA 6 .   ? 79.103  49.563  141.908 1.00 43.71 ? 73   HOH H O     1 
HETATM 10014 O  O     . HOH EA 6 .   ? 86.495  47.006  139.565 1.00 47.30 ? 203  HOH H O     1 
HETATM 10015 O  O     . HOH EA 6 .   ? 79.725  41.939  141.446 1.00 16.31 ? 255  HOH H O     1 
HETATM 10016 O  O     . HOH EA 6 .   ? 78.724  43.516  143.589 1.00 20.82 ? 349  HOH H O     1 
HETATM 10017 O  O     . HOH EA 6 .   ? 89.316  37.274  150.645 1.00 42.66 ? 812  HOH H O     1 
HETATM 10018 O  O     . HOH EA 6 .   ? 91.819  38.236  147.159 1.00 34.28 ? 817  HOH H O     1 
HETATM 10019 O  O     . HOH EA 6 .   ? 94.258  37.813  147.077 1.00 42.16 ? 818  HOH H O     1 
HETATM 10020 O  O     . HOH EA 6 .   ? 92.092  40.440  147.332 1.00 35.17 ? 819  HOH H O     1 
HETATM 10021 O  O     . HOH EA 6 .   ? 79.624  39.306  146.677 1.00 36.52 ? 824  HOH H O     1 
HETATM 10022 O  O     . HOH EA 6 .   ? 80.064  42.118  151.328 1.00 55.35 ? 825  HOH H O     1 
HETATM 10023 O  O     . HOH EA 6 .   ? 88.673  45.922  138.585 1.00 31.10 ? 899  HOH H O     1 
HETATM 10024 O  O     . HOH EA 6 .   ? 85.616  46.142  142.551 1.00 40.89 ? 947  HOH H O     1 
HETATM 10025 O  O     . HOH EA 6 .   ? 86.027  49.045  138.535 1.00 36.31 ? 1068 HOH H O     1 
HETATM 10026 O  O     . HOH EA 6 .   ? 79.420  45.534  147.460 1.00 53.56 ? 1223 HOH H O     1 
HETATM 10027 O  O     . HOH EA 6 .   ? 91.659  38.209  149.709 1.00 47.45 ? 1250 HOH H O     1 
HETATM 10028 O  O     . HOH EA 6 .   ? 91.358  36.006  147.075 1.00 43.64 ? 1251 HOH H O     1 
HETATM 10029 O  O     . HOH EA 6 .   ? 91.381  34.125  148.695 1.00 50.67 ? 1252 HOH H O     1 
HETATM 10030 O  O     . HOH FA 6 .   ? 89.371  38.158  124.366 1.00 31.33 ? 32   HOH L O     1 
HETATM 10031 O  O     . HOH FA 6 .   ? 87.664  51.144  130.743 1.00 14.23 ? 52   HOH L O     1 
HETATM 10032 O  O     . HOH FA 6 .   ? 83.124  49.285  131.613 1.00 16.15 ? 55   HOH L O     1 
HETATM 10033 O  O     . HOH FA 6 .   ? 87.790  31.471  130.859 1.00 22.28 ? 170  HOH L O     1 
HETATM 10034 O  O     . HOH FA 6 .   ? 92.004  36.191  123.116 1.00 29.58 ? 177  HOH L O     1 
HETATM 10035 O  O     . HOH FA 6 .   ? 95.293  35.991  126.182 1.00 38.53 ? 178  HOH L O     1 
HETATM 10036 O  O     . HOH FA 6 .   ? 87.999  40.678  124.497 1.00 20.53 ? 202  HOH L O     1 
HETATM 10037 O  O     . HOH FA 6 .   ? 85.610  26.531  129.415 1.00 26.37 ? 251  HOH L O     1 
HETATM 10038 O  O     . HOH FA 6 .   ? 77.034  30.928  126.333 1.00 26.12 ? 270  HOH L O     1 
HETATM 10039 O  O     . HOH FA 6 .   ? 82.458  46.233  130.433 1.00 20.41 ? 275  HOH L O     1 
HETATM 10040 O  O     . HOH FA 6 .   ? 87.640  34.579  131.122 1.00 16.31 ? 280  HOH L O     1 
HETATM 10041 O  O     . HOH FA 6 .   ? 89.077  36.924  132.352 1.00 19.20 ? 302  HOH L O     1 
HETATM 10042 O  O     . HOH FA 6 .   ? 83.006  23.901  122.270 1.00 60.04 ? 317  HOH L O     1 
HETATM 10043 O  O     . HOH FA 6 .   ? 79.372  48.211  136.832 1.00 24.89 ? 347  HOH L O     1 
HETATM 10044 O  O     . HOH FA 6 .   ? 89.341  40.281  133.093 1.00 16.91 ? 387  HOH L O     1 
HETATM 10045 O  O     . HOH FA 6 .   ? 87.620  32.946  132.677 1.00 19.91 ? 458  HOH L O     1 
HETATM 10046 O  O     . HOH FA 6 .   ? 89.226  34.776  132.704 1.00 20.50 ? 460  HOH L O     1 
HETATM 10047 O  O     . HOH FA 6 .   ? 94.306  37.102  129.410 1.00 31.81 ? 464  HOH L O     1 
HETATM 10048 O  O     . HOH FA 6 .   ? 89.386  29.096  130.440 1.00 34.20 ? 466  HOH L O     1 
HETATM 10049 O  O     . HOH FA 6 .   ? 85.272  31.395  129.956 1.00 20.64 ? 467  HOH L O     1 
HETATM 10050 O  O     . HOH FA 6 .   ? 93.483  33.023  126.980 1.00 42.11 ? 469  HOH L O     1 
HETATM 10051 O  O     . HOH FA 6 .   ? 92.422  31.932  124.973 1.00 36.22 ? 470  HOH L O     1 
HETATM 10052 O  O     . HOH FA 6 .   ? 83.867  32.806  120.451 1.00 36.39 ? 888  HOH L O     1 
HETATM 10053 O  O     . HOH FA 6 .   ? 92.604  36.497  131.697 1.00 36.49 ? 896  HOH L O     1 
HETATM 10054 O  O     . HOH FA 6 .   ? 92.468  28.503  128.317 1.00 51.08 ? 949  HOH L O     1 
HETATM 10055 O  O     . HOH FA 6 .   ? 84.980  22.506  127.652 1.00 45.97 ? 950  HOH L O     1 
HETATM 10056 O  O     . HOH FA 6 .   ? 75.407  21.577  127.770 1.00 37.09 ? 951  HOH L O     1 
HETATM 10057 O  O     . HOH FA 6 .   ? 85.272  26.412  121.041 1.00 33.44 ? 952  HOH L O     1 
HETATM 10058 O  O     . HOH FA 6 .   ? 76.317  29.150  124.800 1.00 48.97 ? 1026 HOH L O     1 
HETATM 10059 O  O     . HOH FA 6 .   ? 88.618  25.470  126.643 1.00 55.93 ? 1073 HOH L O     1 
HETATM 10060 O  O     . HOH FA 6 .   ? 89.683  25.782  128.733 1.00 55.07 ? 1217 HOH L O     1 
HETATM 10061 O  O     . HOH FA 6 .   ? 91.050  34.691  131.379 1.00 31.85 ? 1233 HOH L O     1 
HETATM 10062 O  O     . HOH GA 6 .   ? 95.427  79.369  115.396 1.00 26.88 ? 5556 HOH A O     1 
HETATM 10063 O  O     . HOH GA 6 .   ? 64.778  58.499  118.171 1.00 28.77 ? 5557 HOH A O     1 
HETATM 10064 O  O     . HOH GA 6 .   ? 77.683  79.360  118.216 1.00 17.18 ? 5558 HOH A O     1 
HETATM 10065 O  O     . HOH GA 6 .   ? 52.221  77.295  121.820 1.00 30.53 ? 5559 HOH A O     1 
HETATM 10066 O  O     . HOH GA 6 .   ? 92.741  77.331  122.017 1.00 20.73 ? 5560 HOH A O     1 
HETATM 10067 O  O     . HOH GA 6 .   ? 70.018  59.389  123.377 1.00 15.28 ? 5561 HOH A O     1 
HETATM 10068 O  O     . HOH GA 6 .   ? 52.261  71.872  123.710 1.00 40.05 ? 5562 HOH A O     1 
HETATM 10069 O  O     . HOH GA 6 .   ? 38.338  81.879  124.820 1.00 19.68 ? 5563 HOH A O     1 
HETATM 10070 O  O     . HOH GA 6 .   ? 51.853  78.172  126.095 1.00 18.23 ? 5564 HOH A O     1 
HETATM 10071 O  O     . HOH GA 6 .   ? 73.904  74.809  128.902 1.00 22.74 ? 5565 HOH A O     1 
HETATM 10072 O  O     . HOH GA 6 .   ? 67.751  73.613  132.605 1.00 18.53 ? 5566 HOH A O     1 
HETATM 10073 O  O     . HOH GA 6 .   ? 35.978  94.027  133.816 1.00 25.07 ? 5567 HOH A O     1 
HETATM 10074 O  O     . HOH GA 6 .   ? 67.578  74.596  135.124 1.00 21.49 ? 5568 HOH A O     1 
HETATM 10075 O  O     . HOH GA 6 .   ? 40.408  89.267  135.327 1.00 25.10 ? 5569 HOH A O     1 
HETATM 10076 O  O     . HOH GA 6 .   ? 47.705  65.448  137.510 1.00 28.13 ? 5570 HOH A O     1 
HETATM 10077 O  O     . HOH GA 6 .   ? 60.120  66.079  135.978 1.00 17.87 ? 5571 HOH A O     1 
HETATM 10078 O  O     . HOH GA 6 .   ? 44.832  95.831  138.138 1.00 25.92 ? 5572 HOH A O     1 
HETATM 10079 O  O     . HOH GA 6 .   ? 93.605  63.234  111.233 1.00 31.48 ? 5573 HOH A O     1 
HETATM 10080 O  O     . HOH GA 6 .   ? 84.928  76.411  108.682 1.00 30.89 ? 5574 HOH A O     1 
HETATM 10081 O  O     . HOH GA 6 .   ? 77.759  65.098  113.350 1.00 38.71 ? 5575 HOH A O     1 
HETATM 10082 O  O     . HOH GA 6 .   ? 69.532  63.442  114.575 1.00 26.40 ? 5576 HOH A O     1 
HETATM 10083 O  O     . HOH GA 6 .   ? 80.711  67.827  111.829 1.00 32.45 ? 5577 HOH A O     1 
HETATM 10084 O  O     . HOH GA 6 .   ? 89.548  61.634  108.994 1.00 30.27 ? 5578 HOH A O     1 
HETATM 10085 O  O     . HOH GA 6 .   ? 73.216  69.129  122.520 1.00 30.76 ? 5579 HOH A O     1 
HETATM 10086 O  O     . HOH GA 6 .   ? 77.927  62.616  112.640 1.00 37.59 ? 5580 HOH A O     1 
HETATM 10087 O  O     . HOH GA 6 .   ? 70.310  60.927  112.749 1.00 39.52 ? 5581 HOH A O     1 
HETATM 10088 O  O     . HOH GA 6 .   ? 73.476  64.327  116.301 1.00 35.94 ? 5582 HOH A O     1 
HETATM 10089 O  O     . HOH GA 6 .   ? 73.356  66.218  117.948 1.00 32.15 ? 5583 HOH A O     1 
HETATM 10090 O  O     . HOH GA 6 .   ? 91.962  78.127  119.515 1.00 19.29 ? 5584 HOH A O     1 
HETATM 10091 O  O     . HOH GA 6 .   ? 67.241  85.701  119.056 1.00 28.97 ? 5585 HOH A O     1 
HETATM 10092 O  O     . HOH GA 6 .   ? 75.023  67.479  121.487 1.00 21.87 ? 5586 HOH A O     1 
HETATM 10093 O  O     . HOH GA 6 .   ? 54.790  78.615  120.382 1.00 29.69 ? 5587 HOH A O     1 
HETATM 10094 O  O     . HOH GA 6 .   ? 91.257  85.448  120.934 1.00 29.69 ? 5588 HOH A O     1 
HETATM 10095 O  O     . HOH GA 6 .   ? 48.298  87.075  122.033 1.00 28.41 ? 5589 HOH A O     1 
HETATM 10096 O  O     . HOH GA 6 .   ? 75.219  66.564  119.130 1.00 28.40 ? 5590 HOH A O     1 
HETATM 10097 O  O     . HOH GA 6 .   ? 72.592  71.832  122.922 1.00 21.99 ? 5591 HOH A O     1 
HETATM 10098 O  O     . HOH GA 6 .   ? 53.505  65.290  124.339 1.00 29.07 ? 5592 HOH A O     1 
HETATM 10099 O  O     . HOH GA 6 .   ? 54.844  72.762  123.298 1.00 28.82 ? 5593 HOH A O     1 
HETATM 10100 O  O     . HOH GA 6 .   ? 51.929  67.258  124.204 1.00 34.74 ? 5594 HOH A O     1 
HETATM 10101 O  O     . HOH GA 6 .   ? 83.073  81.397  120.821 1.00 27.63 ? 5595 HOH A O     1 
HETATM 10102 O  O     . HOH GA 6 .   ? 79.268  78.484  125.131 1.00 18.80 ? 5596 HOH A O     1 
HETATM 10103 O  O     . HOH GA 6 .   ? 74.896  84.149  125.870 1.00 27.57 ? 5597 HOH A O     1 
HETATM 10104 O  O     . HOH GA 6 .   ? 70.261  92.555  125.560 1.00 38.06 ? 5598 HOH A O     1 
HETATM 10105 O  O     . HOH GA 6 .   ? 68.235  68.742  130.424 1.00 16.39 ? 5599 HOH A O     1 
HETATM 10106 O  O     . HOH GA 6 .   ? 52.860  94.344  126.138 1.00 33.47 ? 5600 HOH A O     1 
HETATM 10107 O  O     . HOH GA 6 .   ? 54.287  75.634  119.695 1.00 39.37 ? 5601 HOH A O     1 
HETATM 10108 O  O     . HOH GA 6 .   ? 56.835  73.626  125.310 1.00 24.88 ? 5602 HOH A O     1 
HETATM 10109 O  O     . HOH GA 6 .   ? 62.790  92.039  129.739 1.00 29.85 ? 5603 HOH A O     1 
HETATM 10110 O  O     . HOH GA 6 .   ? 59.915  90.773  128.378 1.00 25.56 ? 5604 HOH A O     1 
HETATM 10111 O  O     . HOH GA 6 .   ? 42.738  91.443  131.381 1.00 41.99 ? 5605 HOH A O     1 
HETATM 10112 O  O     . HOH GA 6 .   ? 75.834  70.887  133.481 1.00 23.32 ? 5606 HOH A O     1 
HETATM 10113 O  O     . HOH GA 6 .   ? 69.946  85.166  135.198 1.00 27.27 ? 5607 HOH A O     1 
HETATM 10114 O  O     . HOH GA 6 .   ? 64.271  90.760  123.377 1.00 35.47 ? 5608 HOH A O     1 
HETATM 10115 O  O     . HOH GA 6 .   ? 41.506  91.345  133.773 1.00 22.05 ? 5609 HOH A O     1 
HETATM 10116 O  O     . HOH GA 6 .   ? 58.167  94.252  138.909 1.00 33.79 ? 5610 HOH A O     1 
HETATM 10117 O  O     . HOH GA 6 .   ? 47.336  95.854  133.555 1.00 28.63 ? 5611 HOH A O     1 
HETATM 10118 O  O     . HOH GA 6 .   ? 60.775  71.454  138.427 1.00 22.94 ? 5612 HOH A O     1 
HETATM 10119 O  O     . HOH GA 6 .   ? 38.663  87.163  135.811 1.00 34.66 ? 5613 HOH A O     1 
HETATM 10120 O  O     . HOH GA 6 .   ? 72.964  79.511  136.585 1.00 19.16 ? 5614 HOH A O     1 
HETATM 10121 O  O     . HOH GA 6 .   ? 37.438  80.058  137.480 1.00 25.54 ? 5615 HOH A O     1 
HETATM 10122 O  O     . HOH GA 6 .   ? 59.037  68.025  137.615 1.00 20.27 ? 5616 HOH A O     1 
HETATM 10123 O  O     . HOH GA 6 .   ? 68.288  74.254  137.821 1.00 21.51 ? 5617 HOH A O     1 
HETATM 10124 O  O     . HOH GA 6 .   ? 45.044  80.274  137.902 1.00 20.90 ? 5618 HOH A O     1 
HETATM 10125 O  O     . HOH GA 6 .   ? 70.352  74.807  134.202 1.00 33.85 ? 5619 HOH A O     1 
HETATM 10126 O  O     . HOH GA 6 .   ? 48.954  87.918  140.002 1.00 18.99 ? 5620 HOH A O     1 
HETATM 10127 O  O     . HOH GA 6 .   ? 39.042  82.020  127.594 1.00 20.45 ? 5621 HOH A O     1 
HETATM 10128 O  O     . HOH GA 6 .   ? 39.533  84.208  129.745 1.00 26.56 ? 5622 HOH A O     1 
HETATM 10129 O  O     . HOH GA 6 .   ? 38.191  89.895  127.002 1.00 46.61 ? 5623 HOH A O     1 
HETATM 10130 O  O     . HOH GA 6 .   ? 36.537  87.012  126.850 1.00 52.80 ? 5624 HOH A O     1 
HETATM 10131 O  O     . HOH GA 6 .   ? 34.913  87.406  137.237 1.00 34.97 ? 5625 HOH A O     1 
HETATM 10132 O  O     . HOH GA 6 .   ? 34.084  89.098  142.652 1.00 51.41 ? 5626 HOH A O     1 
HETATM 10133 O  O     . HOH GA 6 .   ? 36.624  89.534  133.181 1.00 26.29 ? 5627 HOH A O     1 
HETATM 10134 O  O     . HOH GA 6 .   ? 41.900  88.881  122.292 1.00 37.62 ? 5628 HOH A O     1 
HETATM 10135 O  O     . HOH GA 6 .   ? 47.343  98.522  131.234 1.00 41.34 ? 5629 HOH A O     1 
HETATM 10136 O  O     . HOH GA 6 .   ? 54.800  97.063  125.957 1.00 49.23 ? 5630 HOH A O     1 
HETATM 10137 O  O     . HOH GA 6 .   ? 47.163  80.419  122.849 1.00 24.50 ? 5631 HOH A O     1 
HETATM 10138 O  O     . HOH GA 6 .   ? 53.289  86.082  119.077 1.00 35.91 ? 5632 HOH A O     1 
HETATM 10139 O  O     . HOH GA 6 .   ? 36.601  82.649  128.523 1.00 40.81 ? 5633 HOH A O     1 
HETATM 10140 O  O     . HOH GA 6 .   ? 35.217  80.766  129.679 1.00 33.73 ? 5634 HOH A O     1 
HETATM 10141 O  O     . HOH GA 6 .   ? 33.298  78.885  129.094 1.00 30.22 ? 5635 HOH A O     1 
HETATM 10142 O  O     . HOH GA 6 .   ? 35.199  81.200  138.396 1.00 29.41 ? 5636 HOH A O     1 
HETATM 10143 O  O     . HOH GA 6 .   ? 44.881  79.351  140.519 1.00 20.26 ? 5637 HOH A O     1 
HETATM 10144 O  O     . HOH GA 6 .   ? 38.318  83.465  137.771 1.00 32.05 ? 5638 HOH A O     1 
HETATM 10145 O  O     . HOH GA 6 .   ? 33.795  78.921  144.615 1.00 36.13 ? 5639 HOH A O     1 
HETATM 10146 O  O     . HOH GA 6 .   ? 58.398  70.297  128.183 1.00 26.77 ? 5640 HOH A O     1 
HETATM 10147 O  O     . HOH GA 6 .   ? 60.011  72.459  128.091 1.00 19.80 ? 5641 HOH A O     1 
HETATM 10148 O  O     . HOH GA 6 .   ? 45.288  65.598  138.544 1.00 32.27 ? 5642 HOH A O     1 
HETATM 10149 O  O     . HOH GA 6 .   ? 45.292  72.608  143.686 1.00 26.87 ? 5643 HOH A O     1 
HETATM 10150 O  O     . HOH GA 6 .   ? 79.763  81.250  117.529 1.00 25.43 ? 5644 HOH A O     1 
HETATM 10151 O  O     . HOH GA 6 .   ? 80.840  79.976  119.844 1.00 27.98 ? 5645 HOH A O     1 
HETATM 10152 O  O     . HOH GA 6 .   ? 54.633  78.585  114.192 1.00 56.75 ? 5646 HOH A O     1 
HETATM 10153 O  O     . HOH GA 6 .   ? 67.060  72.814  139.738 1.00 24.08 ? 5647 HOH A O     1 
HETATM 10154 O  O     . HOH GA 6 .   ? 94.111  71.963  105.984 1.00 40.93 ? 5648 HOH A O     1 
HETATM 10155 O  O     . HOH GA 6 .   ? 72.699  85.589  123.124 1.00 46.47 ? 5649 HOH A O     1 
HETATM 10156 O  O     . HOH GA 6 .   ? 69.964  85.789  123.301 1.00 32.62 ? 5650 HOH A O     1 
HETATM 10157 O  O     . HOH GA 6 .   ? 74.161  85.387  120.186 1.00 30.82 ? 5651 HOH A O     1 
HETATM 10158 O  O     . HOH GA 6 .   ? 57.576  93.846  141.816 1.00 30.67 ? 5652 HOH A O     1 
HETATM 10159 O  O     . HOH GA 6 .   ? 60.450  93.107  138.837 1.00 39.49 ? 5653 HOH A O     1 
HETATM 10160 O  O     . HOH GA 6 .   ? 49.638  99.323  132.245 1.00 42.68 ? 5654 HOH A O     1 
HETATM 10161 O  O     . HOH GA 6 .   ? 41.602  101.167 134.277 1.00 43.40 ? 5655 HOH A O     1 
HETATM 10162 O  O     . HOH GA 6 .   ? 48.201  97.807  135.407 1.00 32.32 ? 5656 HOH A O     1 
HETATM 10163 O  O     . HOH GA 6 .   ? 55.671  61.665  133.224 1.00 22.56 ? 5657 HOH A O     1 
HETATM 10164 O  O     . HOH GA 6 .   ? 54.503  61.711  130.580 1.00 24.21 ? 5658 HOH A O     1 
HETATM 10165 O  O     . HOH GA 6 .   ? 52.360  63.377  130.482 1.00 18.86 ? 5659 HOH A O     1 
HETATM 10166 O  O     . HOH GA 6 .   ? 55.865  61.242  125.823 1.00 26.24 ? 5660 HOH A O     1 
HETATM 10167 O  O     . HOH GA 6 .   ? 84.900  84.804  128.700 1.00 49.01 ? 5661 HOH A O     1 
HETATM 10168 O  O     . HOH GA 6 .   ? 65.100  76.392  143.765 1.00 22.37 ? 5662 HOH A O     1 
HETATM 10169 O  O     . HOH GA 6 .   ? 67.757  76.851  144.419 1.00 40.02 ? 5663 HOH A O     1 
HETATM 10170 O  O     . HOH GA 6 .   ? 42.083  88.260  142.340 1.00 22.97 ? 5664 HOH A O     1 
HETATM 10171 O  O     . HOH GA 6 .   ? 44.139  88.001  130.809 1.00 28.52 ? 5665 HOH A O     1 
HETATM 10172 O  O     . HOH GA 6 .   ? 43.348  84.801  130.062 1.00 24.43 ? 5666 HOH A O     1 
HETATM 10173 O  O     . HOH GA 6 .   ? 48.688  76.449  147.118 1.00 24.72 ? 5667 HOH A O     1 
HETATM 10174 O  O     . HOH GA 6 .   ? 47.053  78.205  147.712 1.00 35.35 ? 5668 HOH A O     1 
HETATM 10175 O  O     . HOH GA 6 .   ? 37.935  95.360  129.273 1.00 43.61 ? 5669 HOH A O     1 
HETATM 10176 O  O     . HOH GA 6 .   ? 39.232  92.323  126.094 1.00 56.67 ? 5670 HOH A O     1 
HETATM 10177 O  O     . HOH GA 6 .   ? 42.323  94.566  127.220 1.00 49.11 ? 5671 HOH A O     1 
HETATM 10178 O  O     . HOH GA 6 .   ? 35.733  96.552  132.873 1.00 39.18 ? 5672 HOH A O     1 
HETATM 10179 O  O     . HOH GA 6 .   ? 37.976  96.024  139.972 1.00 36.87 ? 5673 HOH A O     1 
HETATM 10180 O  O     . HOH GA 6 .   ? 40.041  93.278  128.131 1.00 43.13 ? 5674 HOH A O     1 
HETATM 10181 O  O     . HOH GA 6 .   ? 43.461  99.847  129.244 1.00 47.23 ? 5675 HOH A O     1 
HETATM 10182 O  O     . HOH GA 6 .   ? 52.811  90.674  123.529 1.00 50.51 ? 5676 HOH A O     1 
HETATM 10183 O  O     . HOH GA 6 .   ? 51.173  92.555  124.268 1.00 58.70 ? 5677 HOH A O     1 
HETATM 10184 O  O     . HOH GA 6 .   ? 61.907  92.201  127.264 1.00 47.93 ? 5678 HOH A O     1 
HETATM 10185 O  O     . HOH GA 6 .   ? 59.598  84.602  118.103 1.00 36.75 ? 5679 HOH A O     1 
HETATM 10186 O  O     . HOH GA 6 .   ? 62.356  86.602  121.015 1.00 40.40 ? 5680 HOH A O     1 
HETATM 10187 O  O     . HOH GA 6 .   ? 69.543  86.028  120.702 1.00 33.57 ? 5681 HOH A O     1 
HETATM 10188 O  O     . HOH GA 6 .   ? 76.966  90.134  126.115 1.00 39.92 ? 5682 HOH A O     1 
HETATM 10189 O  O     . HOH GA 6 .   ? 63.228  98.614  134.204 1.00 42.17 ? 5683 HOH A O     1 
HETATM 10190 O  O     . HOH GA 6 .   ? 81.795  85.895  122.297 1.00 46.38 ? 5684 HOH A O     1 
HETATM 10191 O  O     . HOH GA 6 .   ? 79.679  83.672  118.842 1.00 35.83 ? 5685 HOH A O     1 
HETATM 10192 O  O     . HOH GA 6 .   ? 79.021  89.850  127.922 1.00 45.57 ? 5686 HOH A O     1 
HETATM 10193 O  O     . HOH GA 6 .   ? 81.084  89.350  126.042 1.00 46.95 ? 5687 HOH A O     1 
HETATM 10194 O  O     . HOH GA 6 .   ? 87.902  84.408  124.011 1.00 55.49 ? 5688 HOH A O     1 
HETATM 10195 O  O     . HOH GA 6 .   ? 79.774  81.549  114.945 1.00 42.76 ? 5689 HOH A O     1 
HETATM 10196 O  O     . HOH GA 6 .   ? 77.845  80.918  113.778 1.00 48.50 ? 5690 HOH A O     1 
HETATM 10197 O  O     . HOH GA 6 .   ? 81.990  80.956  113.598 1.00 24.65 ? 5691 HOH A O     1 
HETATM 10198 O  O     . HOH GA 6 .   ? 83.251  83.297  112.929 1.00 33.03 ? 5692 HOH A O     1 
HETATM 10199 O  O     . HOH GA 6 .   ? 85.574  83.656  114.413 1.00 32.99 ? 5693 HOH A O     1 
HETATM 10200 O  O     . HOH GA 6 .   ? 74.239  77.142  111.895 1.00 35.78 ? 5694 HOH A O     1 
HETATM 10201 O  O     . HOH GA 6 .   ? 65.346  67.365  109.450 1.00 31.20 ? 5695 HOH A O     1 
HETATM 10202 O  O     . HOH GA 6 .   ? 65.998  77.887  110.962 1.00 57.87 ? 5696 HOH A O     1 
HETATM 10203 O  O     . HOH GA 6 .   ? 64.542  62.127  105.162 1.00 46.98 ? 5697 HOH A O     1 
HETATM 10204 O  O     . HOH GA 6 .   ? 83.453  74.256  111.408 1.00 35.13 ? 5698 HOH A O     1 
HETATM 10205 O  O     . HOH GA 6 .   ? 86.997  78.643  109.066 1.00 23.08 ? 5699 HOH A O     1 
HETATM 10206 O  O     . HOH GA 6 .   ? 84.783  78.664  107.293 1.00 38.25 ? 5700 HOH A O     1 
HETATM 10207 O  O     . HOH GA 6 .   ? 89.980  73.712  108.713 1.00 47.12 ? 5701 HOH A O     1 
HETATM 10208 O  O     . HOH GA 6 .   ? 79.016  80.018  109.696 1.00 54.98 ? 5702 HOH A O     1 
HETATM 10209 O  O     . HOH GA 6 .   ? 96.284  70.448  107.876 1.00 38.58 ? 5703 HOH A O     1 
HETATM 10210 O  O     . HOH GA 6 .   ? 95.053  68.995  104.732 1.00 44.99 ? 5704 HOH A O     1 
HETATM 10211 O  O     . HOH GA 6 .   ? 86.243  61.354  108.983 1.00 39.15 ? 5705 HOH A O     1 
HETATM 10212 O  O     . HOH GA 6 .   ? 89.340  62.777  106.661 1.00 35.44 ? 5706 HOH A O     1 
HETATM 10213 O  O     . HOH GA 6 .   ? 92.122  74.546  109.432 1.00 48.03 ? 5707 HOH A O     1 
HETATM 10214 O  O     . HOH GA 6 .   ? 49.394  65.160  121.033 1.00 37.40 ? 5708 HOH A O     1 
HETATM 10215 O  O     . HOH GA 6 .   ? 55.716  65.949  122.354 1.00 38.30 ? 5709 HOH A O     1 
HETATM 10216 O  O     . HOH GA 6 .   ? 63.611  58.574  130.638 1.00 33.59 ? 5710 HOH A O     1 
HETATM 10217 O  O     . HOH GA 6 .   ? 62.971  60.215  133.387 1.00 39.31 ? 5711 HOH A O     1 
HETATM 10218 O  O     . HOH GA 6 .   ? 50.853  68.954  145.944 1.00 42.70 ? 5712 HOH A O     1 
HETATM 10219 O  O     . HOH GA 6 .   ? 46.516  76.033  146.621 1.00 43.56 ? 5713 HOH A O     1 
HETATM 10220 O  O     . HOH GA 6 .   ? 60.666  61.982  140.644 1.00 30.49 ? 5714 HOH A O     1 
HETATM 10221 O  O     . HOH GA 6 .   ? 63.326  92.424  141.900 1.00 45.31 ? 5715 HOH A O     1 
HETATM 10222 O  O     . HOH GA 6 .   ? 62.245  94.770  141.646 1.00 50.96 ? 5716 HOH A O     1 
HETATM 10223 O  O     . HOH GA 6 .   ? 65.741  84.330  142.416 1.00 20.84 ? 5717 HOH A O     1 
HETATM 10224 O  O     . HOH GA 6 .   ? 60.127  87.735  148.727 1.00 35.04 ? 5718 HOH A O     1 
HETATM 10225 O  O     . HOH GA 6 .   ? 63.700  82.707  151.362 1.00 39.18 ? 5719 HOH A O     1 
HETATM 10226 O  O     . HOH GA 6 .   ? 55.792  89.758  153.298 1.00 39.31 ? 5720 HOH A O     1 
HETATM 10227 O  O     . HOH GA 6 .   ? 53.804  86.345  160.347 1.00 38.03 ? 5721 HOH A O     1 
HETATM 10228 O  O     . HOH GA 6 .   ? 53.476  83.928  161.867 1.00 50.88 ? 5722 HOH A O     1 
HETATM 10229 O  O     . HOH GA 6 .   ? 52.174  88.006  158.228 1.00 27.66 ? 5723 HOH A O     1 
HETATM 10230 O  O     . HOH GA 6 .   ? 55.123  84.578  157.952 1.00 41.60 ? 5724 HOH A O     1 
HETATM 10231 O  O     . HOH GA 6 .   ? 55.206  87.649  157.623 1.00 41.75 ? 5725 HOH A O     1 
HETATM 10232 O  O     . HOH GA 6 .   ? 53.517  86.237  158.176 1.00 27.42 ? 5726 HOH A O     1 
HETATM 10233 O  O     . HOH GA 6 .   ? 57.279  77.226  155.662 1.00 50.42 ? 5727 HOH A O     1 
HETATM 10234 O  O     . HOH GA 6 .   ? 47.653  77.724  152.989 1.00 33.73 ? 5728 HOH A O     1 
HETATM 10235 O  O     . HOH GA 6 .   ? 51.776  71.907  152.305 1.00 37.41 ? 5729 HOH A O     1 
HETATM 10236 O  O     . HOH GA 6 .   ? 56.934  71.363  154.997 1.00 41.50 ? 5730 HOH A O     1 
HETATM 10237 O  O     . HOH GA 6 .   ? 48.546  65.873  118.713 1.00 45.39 ? 5731 HOH A O     1 
HETATM 10238 O  O     . HOH GA 6 .   ? 53.141  49.014  109.150 1.00 54.10 ? 5732 HOH A O     1 
HETATM 10239 O  O     . HOH GA 6 .   ? 57.266  47.472  107.274 1.00 46.28 ? 5733 HOH A O     1 
HETATM 10240 O  O     . HOH GA 6 .   ? 49.301  50.247  111.453 1.00 47.72 ? 5734 HOH A O     1 
HETATM 10241 O  O     . HOH GA 6 .   ? 58.934  46.900  104.948 1.00 51.17 ? 5735 HOH A O     1 
HETATM 10242 O  O     . HOH GA 6 .   ? 68.137  93.582  142.531 1.00 30.94 ? 5736 HOH A O     1 
HETATM 10243 O  O     . HOH GA 6 .   ? 67.146  95.612  143.623 1.00 60.03 ? 5737 HOH A O     1 
HETATM 10244 O  O     . HOH GA 6 .   ? 44.711  76.515  143.443 1.00 35.52 ? 5738 HOH A O     1 
HETATM 10245 O  O     . HOH GA 6 .   ? 44.493  77.195  146.188 1.00 43.13 ? 5739 HOH A O     1 
HETATM 10246 O  O     . HOH GA 6 .   ? 32.654  81.495  130.528 1.00 42.38 ? 5740 HOH A O     1 
HETATM 10247 O  O     . HOH GA 6 .   ? 49.867  79.919  122.428 1.00 38.64 ? 5741 HOH A O     1 
HETATM 10248 O  O     . HOH GA 6 .   ? 51.230  80.620  120.375 1.00 35.44 ? 5742 HOH A O     1 
HETATM 10249 O  O     . HOH GA 6 .   ? 58.272  96.746  137.080 1.00 53.49 ? 5743 HOH A O     1 
HETATM 10250 O  O     . HOH GA 6 .   ? 52.000  100.367 136.852 1.00 52.79 ? 5744 HOH A O     1 
HETATM 10251 O  O     . HOH GA 6 .   ? 43.772  92.771  123.657 1.00 58.83 ? 5745 HOH A O     1 
HETATM 10252 O  O     . HOH GA 6 .   ? 49.568  99.757  134.958 1.00 51.79 ? 5746 HOH A O     1 
HETATM 10253 O  O     . HOH GA 6 .   ? 36.702  87.705  129.426 1.00 47.94 ? 5747 HOH A O     1 
HETATM 10254 O  O     . HOH GA 6 .   ? 55.329  90.645  121.909 1.00 50.55 ? 5748 HOH A O     1 
HETATM 10255 O  O     . HOH GA 6 .   ? 67.045  92.535  122.839 1.00 52.06 ? 5749 HOH A O     1 
HETATM 10256 O  O     . HOH GA 6 .   ? 64.928  94.800  127.574 1.00 44.94 ? 5750 HOH A O     1 
HETATM 10257 O  O     . HOH GA 6 .   ? 77.931  84.944  116.692 1.00 55.62 ? 5751 HOH A O     1 
HETATM 10258 O  O     . HOH GA 6 .   ? 72.688  85.724  117.284 1.00 51.81 ? 5752 HOH A O     1 
HETATM 10259 O  O     . HOH GA 6 .   ? 76.033  86.678  117.914 1.00 58.84 ? 5753 HOH A O     1 
HETATM 10260 O  O     . HOH GA 6 .   ? 68.913  63.089  110.062 1.00 42.66 ? 5754 HOH A O     1 
HETATM 10261 O  O     . HOH GA 6 .   ? 63.053  57.613  105.579 1.00 39.63 ? 5755 HOH A O     1 
HETATM 10262 O  O     . HOH GA 6 .   ? 68.170  72.933  109.703 1.00 45.34 ? 5756 HOH A O     1 
HETATM 10263 O  O     . HOH GA 6 .   ? 61.627  70.000  109.618 1.00 35.93 ? 5757 HOH A O     1 
HETATM 10264 O  O     . HOH GA 6 .   ? 72.061  84.374  114.518 1.00 35.49 ? 5758 HOH A O     1 
HETATM 10265 O  O     . HOH GA 6 .   ? 73.487  74.904  110.134 1.00 36.22 ? 5759 HOH A O     1 
HETATM 10266 O  O     . HOH GA 6 .   ? 84.857  62.941  106.867 1.00 54.13 ? 5760 HOH A O     1 
HETATM 10267 O  O     . HOH GA 6 .   ? 82.022  64.389  108.283 1.00 56.82 ? 5761 HOH A O     1 
HETATM 10268 O  O     . HOH GA 6 .   ? 81.075  70.120  109.211 1.00 49.33 ? 5762 HOH A O     1 
HETATM 10269 O  O     . HOH GA 6 .   ? 57.473  71.090  125.242 1.00 47.93 ? 5763 HOH A O     1 
HETATM 10270 O  O     . HOH GA 6 .   ? 62.107  56.575  120.666 1.00 46.53 ? 5764 HOH A O     1 
HETATM 10271 O  O     . HOH GA 6 .   ? 58.670  62.790  137.823 1.00 32.29 ? 5765 HOH A O     1 
HETATM 10272 O  O     . HOH GA 6 .   ? 58.843  90.882  147.183 1.00 57.51 ? 5766 HOH A O     1 
HETATM 10273 O  O     . HOH GA 6 .   ? 58.756  80.760  156.946 1.00 51.96 ? 5767 HOH A O     1 
HETATM 10274 O  O     . HOH GA 6 .   ? 62.640  93.474  139.493 1.00 51.72 ? 5768 HOH A O     1 
HETATM 10275 O  O     . HOH GA 6 .   ? 58.193  93.220  146.024 1.00 55.93 ? 5769 HOH A O     1 
HETATM 10276 O  O     . HOH GA 6 .   ? 47.065  76.868  155.014 1.00 47.55 ? 5770 HOH A O     1 
HETATM 10277 O  O     . HOH GA 6 .   ? 69.624  74.583  141.237 1.00 37.61 ? 5771 HOH A O     1 
HETATM 10278 O  O     . HOH GA 6 .   ? 70.544  78.246  146.518 1.00 54.50 ? 5772 HOH A O     1 
HETATM 10279 O  O     . HOH GA 6 .   ? 68.013  75.562  151.776 1.00 54.66 ? 5773 HOH A O     1 
HETATM 10280 O  O     . HOH GA 6 .   ? 54.753  69.173  121.166 1.00 47.41 ? 5774 HOH A O     1 
HETATM 10281 O  O     . HOH GA 6 .   ? 50.441  61.150  119.167 1.00 49.86 ? 5775 HOH A O     1 
HETATM 10282 O  O     . HOH GA 6 .   ? 95.166  67.175  107.034 1.00 48.48 ? 5776 HOH A O     1 
HETATM 10283 O  O     . HOH GA 6 .   ? 90.141  83.649  124.035 1.00 30.74 ? 5777 HOH A O     1 
HETATM 10284 O  O     . HOH GA 6 .   ? 86.728  87.541  119.752 1.00 53.37 ? 5778 HOH A O     1 
HETATM 10285 O  O     . HOH GA 6 .   ? 83.804  68.879  109.452 1.00 55.60 ? 5779 HOH A O     1 
HETATM 10286 O  O     . HOH GA 6 .   ? 57.840  97.227  129.518 1.00 38.21 ? 5780 HOH A O     1 
HETATM 10287 O  O     . HOH GA 6 .   ? 55.676  97.751  128.277 1.00 36.76 ? 5781 HOH A O     1 
HETATM 10288 O  O     . HOH GA 6 .   ? 54.209  61.163  123.734 1.00 36.92 ? 5782 HOH A O     1 
HETATM 10289 O  O     . HOH GA 6 .   ? 64.053  94.492  143.532 1.00 48.50 ? 5783 HOH A O     1 
HETATM 10290 O  O     . HOH GA 6 .   ? 56.281  96.172  145.119 1.00 45.70 ? 5784 HOH A O     1 
HETATM 10291 O  O     . HOH GA 6 .   ? 55.860  97.358  137.156 1.00 54.67 ? 5785 HOH A O     1 
HETATM 10292 O  O     . HOH GA 6 .   ? 56.461  95.993  149.882 1.00 54.81 ? 5786 HOH A O     1 
HETATM 10293 O  O     . HOH GA 6 .   ? 43.627  94.210  142.034 1.00 38.83 ? 5787 HOH A O     1 
HETATM 10294 O  O     . HOH GA 6 .   ? 58.269  89.143  120.193 1.00 52.61 ? 5788 HOH A O     1 
HETATM 10295 O  O     . HOH GA 6 .   ? 70.472  82.705  113.105 1.00 51.45 ? 5789 HOH A O     1 
HETATM 10296 O  O     . HOH GA 6 .   ? 78.558  69.028  111.943 1.00 55.35 ? 5790 HOH A O     1 
HETATM 10297 O  O     . HOH GA 6 .   ? 65.921  63.038  108.641 1.00 32.31 ? 5791 HOH A O     1 
HETATM 10298 O  O     . HOH GA 6 .   ? 76.268  74.072  108.405 1.00 38.19 ? 5792 HOH A O     1 
HETATM 10299 O  O     . HOH GA 6 .   ? 90.475  81.589  126.128 1.00 36.85 ? 5793 HOH A O     1 
HETATM 10300 O  O     . HOH GA 6 .   ? 96.432  70.949  105.476 1.00 52.16 ? 5794 HOH A O     1 
HETATM 10301 O  O     . HOH GA 6 .   ? 90.947  72.617  106.670 1.00 46.50 ? 5795 HOH A O     1 
HETATM 10302 O  O     . HOH GA 6 .   ? 82.473  71.718  104.764 1.00 57.10 ? 5796 HOH A O     1 
HETATM 10303 O  O     . HOH GA 6 .   ? 77.097  66.157  120.557 1.00 50.96 ? 5797 HOH A O     1 
HETATM 10304 O  O     . HOH GA 6 .   ? 76.664  72.748  105.540 1.00 53.81 ? 5798 HOH A O     1 
HETATM 10305 O  O     . HOH GA 6 .   ? 49.072  72.921  130.427 1.00 41.06 ? 5799 HOH A O     1 
HETATM 10306 O  O     . HOH GA 6 .   ? 62.851  61.016  131.155 1.00 44.03 ? 5800 HOH A O     1 
HETATM 10307 O  O     . HOH GA 6 .   ? 53.072  66.899  120.295 1.00 55.79 ? 5801 HOH A O     1 
HETATM 10308 O  O     . HOH GA 6 .   ? 64.249  55.920  122.046 1.00 33.81 ? 5802 HOH A O     1 
HETATM 10309 O  O     . HOH GA 6 .   ? 48.097  72.551  149.126 1.00 53.90 ? 5803 HOH A O     1 
HETATM 10310 O  O     . HOH GA 6 .   ? 51.139  93.177  150.462 1.00 45.37 ? 5804 HOH A O     1 
HETATM 10311 O  O     . HOH GA 6 .   ? 58.771  73.315  153.750 1.00 35.28 ? 5805 HOH A O     1 
HETATM 10312 O  O     . HOH GA 6 .   ? 74.992  85.976  124.213 1.00 59.54 ? 5806 HOH A O     1 
HETATM 10313 O  O     . HOH GA 6 .   ? 99.390  76.121  120.732 1.00 41.44 ? 5807 HOH A O     1 
HETATM 10314 O  O     . HOH GA 6 .   ? 41.128  78.736  149.256 1.00 40.71 ? 5808 HOH A O     1 
HETATM 10315 O  O     . HOH GA 6 .   ? 43.761  85.223  132.175 1.00 45.93 ? 5809 HOH A O     1 
HETATM 10316 O  O     . HOH GA 6 .   ? 60.486  85.593  119.975 1.00 54.01 ? 5810 HOH A O     1 
HETATM 10317 O  O     . HOH GA 6 .   ? 55.364  60.172  118.687 1.00 47.02 ? 5811 HOH A O     1 
HETATM 10318 O  O     . HOH GA 6 .   ? 64.809  78.622  153.536 1.00 48.79 ? 5812 HOH A O     1 
HETATM 10319 O  O     . HOH GA 6 .   ? 62.943  70.713  149.623 1.00 35.85 ? 5813 HOH A O     1 
HETATM 10320 O  O     . HOH HA 6 .   ? 27.090  67.511  115.873 1.00 26.02 ? 3334 HOH B O     1 
HETATM 10321 O  O     . HOH HA 6 .   ? 35.834  45.257  118.062 1.00 25.40 ? 3335 HOH B O     1 
HETATM 10322 O  O     . HOH HA 6 .   ? 32.041  75.843  120.053 1.00 52.95 ? 3336 HOH B O     1 
HETATM 10323 O  O     . HOH HA 6 .   ? 28.688  61.085  118.845 1.00 25.40 ? 3337 HOH B O     1 
HETATM 10324 O  O     . HOH HA 6 .   ? 23.402  67.921  124.081 1.00 22.59 ? 3338 HOH B O     1 
HETATM 10325 O  O     . HOH HA 6 .   ? 52.361  50.572  125.393 1.00 17.28 ? 3339 HOH B O     1 
HETATM 10326 O  O     . HOH HA 6 .   ? 20.153  61.552  125.017 1.00 29.01 ? 3340 HOH B O     1 
HETATM 10327 O  O     . HOH HA 6 .   ? 45.592  46.039  128.740 1.00 19.62 ? 3341 HOH B O     1 
HETATM 10328 O  O     . HOH HA 6 .   ? 45.355  40.009  132.858 1.00 20.52 ? 3342 HOH B O     1 
HETATM 10329 O  O     . HOH HA 6 .   ? 31.919  52.371  141.303 1.00 35.03 ? 3343 HOH B O     1 
HETATM 10330 O  O     . HOH HA 6 .   ? 30.970  73.569  133.565 1.00 20.08 ? 3344 HOH B O     1 
HETATM 10331 O  O     . HOH HA 6 .   ? 40.659  61.592  138.023 1.00 27.48 ? 3345 HOH B O     1 
HETATM 10332 O  O     . HOH HA 6 .   ? 59.298  47.111  139.134 1.00 15.84 ? 3346 HOH B O     1 
HETATM 10333 O  O     . HOH HA 6 .   ? 40.225  63.133  112.605 1.00 28.46 ? 3347 HOH B O     1 
HETATM 10334 O  O     . HOH HA 6 .   ? 20.704  51.574  122.043 1.00 60.03 ? 3348 HOH B O     1 
HETATM 10335 O  O     . HOH HA 6 .   ? 43.327  47.371  117.406 1.00 25.32 ? 3349 HOH B O     1 
HETATM 10336 O  O     . HOH HA 6 .   ? 46.919  52.878  122.394 1.00 23.99 ? 3350 HOH B O     1 
HETATM 10337 O  O     . HOH HA 6 .   ? 17.209  61.168  126.867 1.00 42.34 ? 3351 HOH B O     1 
HETATM 10338 O  O     . HOH HA 6 .   ? 26.890  40.788  117.504 1.00 33.56 ? 3352 HOH B O     1 
HETATM 10339 O  O     . HOH HA 6 .   ? 18.512  63.958  117.520 1.00 38.82 ? 3353 HOH B O     1 
HETATM 10340 O  O     . HOH HA 6 .   ? 21.087  61.644  116.485 1.00 33.95 ? 3354 HOH B O     1 
HETATM 10341 O  O     . HOH HA 6 .   ? 36.250  66.762  118.677 1.00 21.74 ? 3355 HOH B O     1 
HETATM 10342 O  O     . HOH HA 6 .   ? 56.518  54.953  121.039 1.00 36.66 ? 3356 HOH B O     1 
HETATM 10343 O  O     . HOH HA 6 .   ? 20.017  63.379  119.861 1.00 27.50 ? 3357 HOH B O     1 
HETATM 10344 O  O     . HOH HA 6 .   ? 15.780  64.324  117.320 1.00 60.04 ? 3358 HOH B O     1 
HETATM 10345 O  O     . HOH HA 6 .   ? 33.703  73.950  121.074 1.00 27.54 ? 3359 HOH B O     1 
HETATM 10346 O  O     . HOH HA 6 .   ? 35.371  66.627  121.240 1.00 23.33 ? 3360 HOH B O     1 
HETATM 10347 O  O     . HOH HA 6 .   ? 50.045  66.991  122.604 1.00 44.53 ? 3361 HOH B O     1 
HETATM 10348 O  O     . HOH HA 6 .   ? 27.089  71.452  122.339 1.00 28.28 ? 3362 HOH B O     1 
HETATM 10349 O  O     . HOH HA 6 .   ? 19.184  60.557  122.895 1.00 26.95 ? 3363 HOH B O     1 
HETATM 10350 O  O     . HOH HA 6 .   ? 26.912  66.260  127.845 1.00 31.24 ? 3364 HOH B O     1 
HETATM 10351 O  O     . HOH HA 6 .   ? 25.341  69.426  122.637 1.00 23.78 ? 3365 HOH B O     1 
HETATM 10352 O  O     . HOH HA 6 .   ? 24.519  73.050  124.212 1.00 26.43 ? 3366 HOH B O     1 
HETATM 10353 O  O     . HOH HA 6 .   ? 49.447  69.271  121.620 1.00 33.34 ? 3367 HOH B O     1 
HETATM 10354 O  O     . HOH HA 6 .   ? 41.147  39.445  124.946 1.00 21.17 ? 3368 HOH B O     1 
HETATM 10355 O  O     . HOH HA 6 .   ? 51.850  54.868  125.367 1.00 18.26 ? 3369 HOH B O     1 
HETATM 10356 O  O     . HOH HA 6 .   ? 49.845  55.370  123.491 1.00 21.01 ? 3370 HOH B O     1 
HETATM 10357 O  O     . HOH HA 6 .   ? 44.920  45.822  126.150 1.00 20.05 ? 3371 HOH B O     1 
HETATM 10358 O  O     . HOH HA 6 .   ? 44.904  54.152  132.720 1.00 19.83 ? 3372 HOH B O     1 
HETATM 10359 O  O     . HOH HA 6 .   ? 23.310  66.778  126.621 1.00 34.85 ? 3373 HOH B O     1 
HETATM 10360 O  O     . HOH HA 6 .   ? 47.397  73.599  127.635 1.00 21.06 ? 3374 HOH B O     1 
HETATM 10361 O  O     . HOH HA 6 .   ? 29.811  67.736  128.485 1.00 23.99 ? 3375 HOH B O     1 
HETATM 10362 O  O     . HOH HA 6 .   ? 57.537  53.448  129.015 1.00 34.34 ? 3376 HOH B O     1 
HETATM 10363 O  O     . HOH HA 6 .   ? 48.044  66.586  130.146 1.00 36.38 ? 3377 HOH B O     1 
HETATM 10364 O  O     . HOH HA 6 .   ? 48.812  37.041  130.558 1.00 20.86 ? 3378 HOH B O     1 
HETATM 10365 O  O     . HOH HA 6 .   ? 31.487  31.870  133.246 1.00 38.02 ? 3379 HOH B O     1 
HETATM 10366 O  O     . HOH HA 6 .   ? 31.281  72.720  130.849 1.00 20.41 ? 3380 HOH B O     1 
HETATM 10367 O  O     . HOH HA 6 .   ? 34.153  65.357  136.432 1.00 22.47 ? 3381 HOH B O     1 
HETATM 10368 O  O     . HOH HA 6 .   ? 26.596  47.295  129.969 1.00 33.53 ? 3382 HOH B O     1 
HETATM 10369 O  O     . HOH HA 6 .   ? 27.025  50.400  131.414 1.00 30.20 ? 3383 HOH B O     1 
HETATM 10370 O  O     . HOH HA 6 .   ? 42.949  57.414  135.187 1.00 24.71 ? 3384 HOH B O     1 
HETATM 10371 O  O     . HOH HA 6 .   ? 45.586  45.016  123.559 1.00 23.89 ? 3385 HOH B O     1 
HETATM 10372 O  O     . HOH HA 6 .   ? 50.397  46.627  131.292 1.00 17.00 ? 3386 HOH B O     1 
HETATM 10373 O  O     . HOH HA 6 .   ? 42.883  62.170  139.674 1.00 39.46 ? 3387 HOH B O     1 
HETATM 10374 O  O     . HOH HA 6 .   ? 27.755  63.003  136.784 1.00 31.53 ? 3388 HOH B O     1 
HETATM 10375 O  O     . HOH HA 6 .   ? 35.407  63.133  137.459 1.00 34.50 ? 3389 HOH B O     1 
HETATM 10376 O  O     . HOH HA 6 .   ? 37.609  61.100  133.693 1.00 20.47 ? 3390 HOH B O     1 
HETATM 10377 O  O     . HOH HA 6 .   ? 27.126  40.156  134.618 1.00 36.44 ? 3391 HOH B O     1 
HETATM 10378 O  O     . HOH HA 6 .   ? 45.031  43.139  127.185 1.00 32.53 ? 3392 HOH B O     1 
HETATM 10379 O  O     . HOH HA 6 .   ? 46.970  55.259  135.048 1.00 37.47 ? 3393 HOH B O     1 
HETATM 10380 O  O     . HOH HA 6 .   ? 46.773  56.065  132.686 1.00 28.17 ? 3394 HOH B O     1 
HETATM 10381 O  O     . HOH HA 6 .   ? 54.747  60.647  135.469 1.00 28.43 ? 3395 HOH B O     1 
HETATM 10382 O  O     . HOH HA 6 .   ? 50.220  62.131  136.587 1.00 27.39 ? 3396 HOH B O     1 
HETATM 10383 O  O     . HOH HA 6 .   ? 34.350  61.589  139.089 1.00 35.67 ? 3397 HOH B O     1 
HETATM 10384 O  O     . HOH HA 6 .   ? 47.942  63.209  136.232 1.00 29.58 ? 3398 HOH B O     1 
HETATM 10385 O  O     . HOH HA 6 .   ? 42.507  34.258  136.923 1.00 19.23 ? 3399 HOH B O     1 
HETATM 10386 O  O     . HOH HA 6 .   ? 52.166  63.954  137.224 1.00 25.34 ? 3400 HOH B O     1 
HETATM 10387 O  O     . HOH HA 6 .   ? 54.884  43.443  134.639 1.00 15.44 ? 3401 HOH B O     1 
HETATM 10388 O  O     . HOH HA 6 .   ? 38.125  61.300  137.996 1.00 28.18 ? 3402 HOH B O     1 
HETATM 10389 O  O     . HOH HA 6 .   ? 43.038  59.475  137.304 1.00 26.15 ? 3403 HOH B O     1 
HETATM 10390 O  O     . HOH HA 6 .   ? 23.851  75.586  127.105 1.00 44.51 ? 3404 HOH B O     1 
HETATM 10391 O  O     . HOH HA 6 .   ? 29.494  71.778  128.766 1.00 24.07 ? 3405 HOH B O     1 
HETATM 10392 O  O     . HOH HA 6 .   ? 25.716  73.826  127.531 1.00 43.84 ? 3406 HOH B O     1 
HETATM 10393 O  O     . HOH HA 6 .   ? 24.758  69.018  135.852 1.00 41.16 ? 3407 HOH B O     1 
HETATM 10394 O  O     . HOH HA 6 .   ? 36.089  60.414  140.024 1.00 57.13 ? 3408 HOH B O     1 
HETATM 10395 O  O     . HOH HA 6 .   ? 27.117  74.157  120.967 1.00 38.98 ? 3409 HOH B O     1 
HETATM 10396 O  O     . HOH HA 6 .   ? 49.013  66.614  139.521 1.00 31.45 ? 3410 HOH B O     1 
HETATM 10397 O  O     . HOH HA 6 .   ? 45.583  67.859  145.471 1.00 37.41 ? 3411 HOH B O     1 
HETATM 10398 O  O     . HOH HA 6 .   ? 59.856  28.303  154.557 1.00 33.02 ? 3412 HOH B O     1 
HETATM 10399 O  O     . HOH HA 6 .   ? 58.456  28.576  157.056 1.00 44.21 ? 3413 HOH B O     1 
HETATM 10400 O  O     . HOH HA 6 .   ? 59.171  23.963  152.524 1.00 45.52 ? 3414 HOH B O     1 
HETATM 10401 O  O     . HOH HA 6 .   ? 34.947  41.598  125.475 1.00 35.00 ? 3415 HOH B O     1 
HETATM 10402 O  O     . HOH HA 6 .   ? 52.123  40.754  140.873 1.00 19.26 ? 3416 HOH B O     1 
HETATM 10403 O  O     . HOH HA 6 .   ? 54.292  40.536  146.659 1.00 28.40 ? 3417 HOH B O     1 
HETATM 10404 O  O     . HOH HA 6 .   ? 52.960  41.078  143.227 1.00 25.98 ? 3418 HOH B O     1 
HETATM 10405 O  O     . HOH HA 6 .   ? 52.870  43.054  144.383 1.00 31.03 ? 3419 HOH B O     1 
HETATM 10406 O  O     . HOH HA 6 .   ? 50.258  42.215  139.650 1.00 22.88 ? 3420 HOH B O     1 
HETATM 10407 O  O     . HOH HA 6 .   ? 47.594  42.209  138.823 1.00 20.55 ? 3421 HOH B O     1 
HETATM 10408 O  O     . HOH HA 6 .   ? 26.188  48.162  132.225 1.00 45.12 ? 3422 HOH B O     1 
HETATM 10409 O  O     . HOH HA 6 .   ? 46.956  46.399  121.716 1.00 25.32 ? 3423 HOH B O     1 
HETATM 10410 O  O     . HOH HA 6 .   ? 54.297  62.440  137.449 1.00 31.91 ? 3424 HOH B O     1 
HETATM 10411 O  O     . HOH HA 6 .   ? 54.977  60.294  128.180 1.00 23.83 ? 3425 HOH B O     1 
HETATM 10412 O  O     . HOH HA 6 .   ? 54.498  58.807  122.051 1.00 49.16 ? 3426 HOH B O     1 
HETATM 10413 O  O     . HOH HA 6 .   ? 50.059  59.989  138.571 1.00 27.09 ? 3427 HOH B O     1 
HETATM 10414 O  O     . HOH HA 6 .   ? 26.971  59.148  138.210 1.00 57.60 ? 3428 HOH B O     1 
HETATM 10415 O  O     . HOH HA 6 .   ? 56.218  55.708  129.136 1.00 54.92 ? 3429 HOH B O     1 
HETATM 10416 O  O     . HOH HA 6 .   ? 56.227  63.036  139.551 1.00 37.63 ? 3430 HOH B O     1 
HETATM 10417 O  O     . HOH HA 6 .   ? 54.980  64.461  141.178 1.00 42.37 ? 3431 HOH B O     1 
HETATM 10418 O  O     . HOH HA 6 .   ? 56.593  62.828  148.365 1.00 40.46 ? 3432 HOH B O     1 
HETATM 10419 O  O     . HOH HA 6 .   ? 41.832  62.554  146.598 1.00 51.21 ? 3433 HOH B O     1 
HETATM 10420 O  O     . HOH HA 6 .   ? 57.011  59.123  136.430 1.00 39.04 ? 3434 HOH B O     1 
HETATM 10421 O  O     . HOH HA 6 .   ? 61.787  56.789  138.030 1.00 45.59 ? 3435 HOH B O     1 
HETATM 10422 O  O     . HOH HA 6 .   ? 21.928  52.573  120.289 1.00 60.04 ? 3436 HOH B O     1 
HETATM 10423 O  O     . HOH HA 6 .   ? 18.620  54.461  121.211 1.00 46.38 ? 3437 HOH B O     1 
HETATM 10424 O  O     . HOH HA 6 .   ? 24.058  50.803  120.206 1.00 38.08 ? 3438 HOH B O     1 
HETATM 10425 O  O     . HOH HA 6 .   ? 24.519  51.004  117.432 1.00 46.05 ? 3439 HOH B O     1 
HETATM 10426 O  O     . HOH HA 6 .   ? 21.995  57.183  132.677 1.00 36.89 ? 3440 HOH B O     1 
HETATM 10427 O  O     . HOH HA 6 .   ? 33.890  46.848  110.163 1.00 50.78 ? 3441 HOH B O     1 
HETATM 10428 O  O     . HOH HA 6 .   ? 22.881  68.002  113.713 1.00 37.00 ? 3442 HOH B O     1 
HETATM 10429 O  O     . HOH HA 6 .   ? 15.636  62.007  114.870 1.00 53.05 ? 3443 HOH B O     1 
HETATM 10430 O  O     . HOH HA 6 .   ? 17.968  59.195  115.084 1.00 50.20 ? 3444 HOH B O     1 
HETATM 10431 O  O     . HOH HA 6 .   ? 15.799  54.450  115.242 1.00 49.61 ? 3445 HOH B O     1 
HETATM 10432 O  O     . HOH HA 6 .   ? 19.413  72.492  122.956 1.00 43.62 ? 3446 HOH B O     1 
HETATM 10433 O  O     . HOH HA 6 .   ? 15.058  73.463  122.186 1.00 49.04 ? 3447 HOH B O     1 
HETATM 10434 O  O     . HOH HA 6 .   ? 16.739  72.014  123.867 1.00 44.82 ? 3448 HOH B O     1 
HETATM 10435 O  O     . HOH HA 6 .   ? 13.810  65.581  122.726 1.00 29.09 ? 3449 HOH B O     1 
HETATM 10436 O  O     . HOH HA 6 .   ? 18.356  71.358  127.735 1.00 34.75 ? 3450 HOH B O     1 
HETATM 10437 O  O     . HOH HA 6 .   ? 40.050  65.282  112.881 1.00 45.41 ? 3451 HOH B O     1 
HETATM 10438 O  O     . HOH HA 6 .   ? 26.883  63.558  109.702 1.00 37.36 ? 3452 HOH B O     1 
HETATM 10439 O  O     . HOH HA 6 .   ? 39.290  65.479  103.825 1.00 41.32 ? 3453 HOH B O     1 
HETATM 10440 O  O     . HOH HA 6 .   ? 39.812  63.530  106.764 1.00 36.60 ? 3454 HOH B O     1 
HETATM 10441 O  O     . HOH HA 6 .   ? 40.799  65.048  108.701 1.00 48.75 ? 3455 HOH B O     1 
HETATM 10442 O  O     . HOH HA 6 .   ? 42.527  63.463  110.477 1.00 44.70 ? 3456 HOH B O     1 
HETATM 10443 O  O     . HOH HA 6 .   ? 42.741  67.438  116.070 1.00 32.40 ? 3457 HOH B O     1 
HETATM 10444 O  O     . HOH HA 6 .   ? 24.638  61.274  109.516 1.00 50.04 ? 3458 HOH B O     1 
HETATM 10445 O  O     . HOH HA 6 .   ? 12.189  60.999  120.249 1.00 21.57 ? 3459 HOH B O     1 
HETATM 10446 O  O     . HOH HA 6 .   ? 13.242  61.472  116.077 1.00 32.97 ? 3460 HOH B O     1 
HETATM 10447 O  O     . HOH HA 6 .   ? 13.226  64.705  120.292 1.00 38.83 ? 3461 HOH B O     1 
HETATM 10448 O  O     . HOH HA 6 .   ? 13.227  60.610  122.857 1.00 23.47 ? 3462 HOH B O     1 
HETATM 10449 O  O     . HOH HA 6 .   ? 13.921  62.956  123.932 1.00 37.05 ? 3463 HOH B O     1 
HETATM 10450 O  O     . HOH HA 6 .   ? 20.906  69.423  129.673 1.00 46.31 ? 3464 HOH B O     1 
HETATM 10451 O  O     . HOH HA 6 .   ? 29.379  58.560  140.314 1.00 41.09 ? 3465 HOH B O     1 
HETATM 10452 O  O     . HOH HA 6 .   ? 30.228  54.465  140.573 1.00 39.43 ? 3466 HOH B O     1 
HETATM 10453 O  O     . HOH HA 6 .   ? 32.577  45.018  141.474 1.00 28.93 ? 3467 HOH B O     1 
HETATM 10454 O  O     . HOH HA 6 .   ? 33.011  42.469  140.017 1.00 38.58 ? 3468 HOH B O     1 
HETATM 10455 O  O     . HOH HA 6 .   ? 33.423  41.960  137.297 1.00 31.24 ? 3469 HOH B O     1 
HETATM 10456 O  O     . HOH HA 6 .   ? 27.629  46.562  136.812 1.00 37.32 ? 3470 HOH B O     1 
HETATM 10457 O  O     . HOH HA 6 .   ? 25.259  47.011  135.634 1.00 56.68 ? 3471 HOH B O     1 
HETATM 10458 O  O     . HOH HA 6 .   ? 36.130  37.324  135.360 1.00 27.73 ? 3472 HOH B O     1 
HETATM 10459 O  O     . HOH HA 6 .   ? 31.054  33.999  134.797 1.00 42.68 ? 3473 HOH B O     1 
HETATM 10460 O  O     . HOH HA 6 .   ? 34.005  39.312  138.002 1.00 38.89 ? 3474 HOH B O     1 
HETATM 10461 O  O     . HOH HA 6 .   ? 34.380  38.139  140.925 1.00 30.99 ? 3475 HOH B O     1 
HETATM 10462 O  O     . HOH HA 6 .   ? 35.981  32.868  139.655 1.00 47.82 ? 3476 HOH B O     1 
HETATM 10463 O  O     . HOH HA 6 .   ? 40.820  36.071  143.593 1.00 23.47 ? 3477 HOH B O     1 
HETATM 10464 O  O     . HOH HA 6 .   ? 39.172  28.581  130.312 1.00 35.55 ? 3478 HOH B O     1 
HETATM 10465 O  O     . HOH HA 6 .   ? 31.137  36.306  138.493 1.00 50.83 ? 3479 HOH B O     1 
HETATM 10466 O  O     . HOH HA 6 .   ? 40.741  32.747  142.209 1.00 36.39 ? 3480 HOH B O     1 
HETATM 10467 O  O     . HOH HA 6 .   ? 37.924  26.914  141.552 1.00 46.63 ? 3481 HOH B O     1 
HETATM 10468 O  O     . HOH HA 6 .   ? 39.700  32.108  147.834 1.00 31.28 ? 3482 HOH B O     1 
HETATM 10469 O  O     . HOH HA 6 .   ? 37.442  30.320  148.170 1.00 56.01 ? 3483 HOH B O     1 
HETATM 10470 O  O     . HOH HA 6 .   ? 39.516  33.748  144.513 1.00 32.59 ? 3484 HOH B O     1 
HETATM 10471 O  O     . HOH HA 6 .   ? 36.510  33.489  143.613 1.00 43.87 ? 3485 HOH B O     1 
HETATM 10472 O  O     . HOH HA 6 .   ? 37.773  25.211  139.965 1.00 45.91 ? 3486 HOH B O     1 
HETATM 10473 O  O     . HOH HA 6 .   ? 37.058  36.034  147.971 1.00 37.74 ? 3487 HOH B O     1 
HETATM 10474 O  O     . HOH HA 6 .   ? 39.357  34.803  147.054 1.00 44.24 ? 3488 HOH B O     1 
HETATM 10475 O  O     . HOH HA 6 .   ? 33.159  39.668  143.009 1.00 51.37 ? 3489 HOH B O     1 
HETATM 10476 O  O     . HOH HA 6 .   ? 35.495  43.529  147.447 1.00 60.04 ? 3490 HOH B O     1 
HETATM 10477 O  O     . HOH HA 6 .   ? 42.104  40.320  149.552 1.00 34.63 ? 3491 HOH B O     1 
HETATM 10478 O  O     . HOH HA 6 .   ? 40.308  37.312  150.752 1.00 54.79 ? 3492 HOH B O     1 
HETATM 10479 O  O     . HOH HA 6 .   ? 36.975  49.669  148.004 1.00 49.88 ? 3493 HOH B O     1 
HETATM 10480 O  O     . HOH HA 6 .   ? 32.879  48.600  144.373 1.00 54.64 ? 3494 HOH B O     1 
HETATM 10481 O  O     . HOH HA 6 .   ? 49.480  51.054  152.033 1.00 35.08 ? 3495 HOH B O     1 
HETATM 10482 O  O     . HOH HA 6 .   ? 46.153  54.200  151.556 1.00 38.83 ? 3496 HOH B O     1 
HETATM 10483 O  O     . HOH HA 6 .   ? 54.480  47.493  147.620 1.00 30.40 ? 3497 HOH B O     1 
HETATM 10484 O  O     . HOH HA 6 .   ? 53.791  51.397  153.172 1.00 35.98 ? 3498 HOH B O     1 
HETATM 10485 O  O     . HOH HA 6 .   ? 52.171  35.724  150.771 1.00 41.02 ? 3499 HOH B O     1 
HETATM 10486 O  O     . HOH HA 6 .   ? 46.653  51.536  152.713 1.00 47.89 ? 3500 HOH B O     1 
HETATM 10487 O  O     . HOH HA 6 .   ? 50.886  37.742  149.942 1.00 58.16 ? 3501 HOH B O     1 
HETATM 10488 O  O     . HOH HA 6 .   ? 54.505  38.849  149.430 1.00 35.03 ? 3502 HOH B O     1 
HETATM 10489 O  O     . HOH HA 6 .   ? 56.355  47.022  149.347 1.00 41.73 ? 3503 HOH B O     1 
HETATM 10490 O  O     . HOH HA 6 .   ? 52.581  31.272  154.359 1.00 49.69 ? 3504 HOH B O     1 
HETATM 10491 O  O     . HOH HA 6 .   ? 58.757  52.688  143.929 1.00 26.48 ? 3505 HOH B O     1 
HETATM 10492 O  O     . HOH HA 6 .   ? 45.466  56.738  135.977 1.00 42.94 ? 3506 HOH B O     1 
HETATM 10493 O  O     . HOH HA 6 .   ? 49.368  57.108  138.610 1.00 44.95 ? 3507 HOH B O     1 
HETATM 10494 O  O     . HOH HA 6 .   ? 46.178  32.216  151.126 1.00 31.97 ? 3508 HOH B O     1 
HETATM 10495 O  O     . HOH HA 6 .   ? 48.408  26.645  154.387 1.00 29.57 ? 3509 HOH B O     1 
HETATM 10496 O  O     . HOH HA 6 .   ? 47.873  24.058  153.655 1.00 27.36 ? 3510 HOH B O     1 
HETATM 10497 O  O     . HOH HA 6 .   ? 44.818  22.191  143.692 1.00 18.14 ? 3511 HOH B O     1 
HETATM 10498 O  O     . HOH HA 6 .   ? 46.109  21.452  141.289 1.00 23.62 ? 3512 HOH B O     1 
HETATM 10499 O  O     . HOH HA 6 .   ? 37.002  20.480  142.312 1.00 48.57 ? 3513 HOH B O     1 
HETATM 10500 O  O     . HOH HA 6 .   ? 38.943  22.807  139.885 1.00 36.97 ? 3514 HOH B O     1 
HETATM 10501 O  O     . HOH HA 6 .   ? 47.693  15.744  146.773 1.00 46.22 ? 3515 HOH B O     1 
HETATM 10502 O  O     . HOH HA 6 .   ? 48.312  15.008  142.919 1.00 39.12 ? 3516 HOH B O     1 
HETATM 10503 O  O     . HOH HA 6 .   ? 47.514  18.896  138.395 1.00 37.50 ? 3517 HOH B O     1 
HETATM 10504 O  O     . HOH HA 6 .   ? 52.027  20.553  155.940 1.00 37.94 ? 3518 HOH B O     1 
HETATM 10505 O  O     . HOH HA 6 .   ? 56.840  27.668  159.959 1.00 58.33 ? 3519 HOH B O     1 
HETATM 10506 O  O     . HOH HA 6 .   ? 59.365  31.706  154.689 1.00 32.00 ? 3520 HOH B O     1 
HETATM 10507 O  O     . HOH HA 6 .   ? 54.948  24.518  160.468 1.00 53.82 ? 3521 HOH B O     1 
HETATM 10508 O  O     . HOH HA 6 .   ? 55.655  22.066  156.415 1.00 36.23 ? 3522 HOH B O     1 
HETATM 10509 O  O     . HOH HA 6 .   ? 48.077  22.780  155.711 1.00 43.09 ? 3523 HOH B O     1 
HETATM 10510 O  O     . HOH HA 6 .   ? 52.420  40.204  149.557 1.00 54.34 ? 3524 HOH B O     1 
HETATM 10511 O  O     . HOH HA 6 .   ? 39.362  44.873  148.259 1.00 48.20 ? 3525 HOH B O     1 
HETATM 10512 O  O     . HOH HA 6 .   ? 54.953  56.934  123.759 1.00 34.59 ? 3526 HOH B O     1 
HETATM 10513 O  O     . HOH HA 6 .   ? 54.887  61.432  141.826 1.00 45.53 ? 3527 HOH B O     1 
HETATM 10514 O  O     . HOH HA 6 .   ? 57.554  58.217  138.700 1.00 52.78 ? 3528 HOH B O     1 
HETATM 10515 O  O     . HOH HA 6 .   ? 61.375  53.751  140.147 1.00 38.55 ? 3529 HOH B O     1 
HETATM 10516 O  O     . HOH HA 6 .   ? 58.014  53.848  122.943 1.00 46.06 ? 3530 HOH B O     1 
HETATM 10517 O  O     . HOH HA 6 .   ? 29.341  54.024  105.788 1.00 60.03 ? 3531 HOH B O     1 
HETATM 10518 O  O     . HOH HA 6 .   ? 48.186  44.011  120.522 1.00 40.95 ? 3532 HOH B O     1 
HETATM 10519 O  O     . HOH HA 6 .   ? 45.778  43.022  120.205 1.00 43.11 ? 3533 HOH B O     1 
HETATM 10520 O  O     . HOH HA 6 .   ? 35.558  47.432  112.193 1.00 60.04 ? 3534 HOH B O     1 
HETATM 10521 O  O     . HOH HA 6 .   ? 25.855  61.333  106.445 1.00 60.04 ? 3535 HOH B O     1 
HETATM 10522 O  O     . HOH HA 6 .   ? 35.359  65.210  102.392 1.00 54.48 ? 3536 HOH B O     1 
HETATM 10523 O  O     . HOH HA 6 .   ? 35.277  56.544  101.802 1.00 42.71 ? 3537 HOH B O     1 
HETATM 10524 O  O     . HOH HA 6 .   ? 38.563  64.470  111.396 1.00 54.26 ? 3538 HOH B O     1 
HETATM 10525 O  O     . HOH HA 6 .   ? 46.082  60.976  107.789 1.00 48.80 ? 3539 HOH B O     1 
HETATM 10526 O  O     . HOH HA 6 .   ? 40.741  63.734  104.230 1.00 53.18 ? 3540 HOH B O     1 
HETATM 10527 O  O     . HOH HA 6 .   ? 45.769  53.449  107.173 1.00 38.67 ? 3541 HOH B O     1 
HETATM 10528 O  O     . HOH HA 6 .   ? 43.992  44.735  117.501 1.00 44.50 ? 3542 HOH B O     1 
HETATM 10529 O  O     . HOH HA 6 .   ? 41.749  32.563  140.240 1.00 57.18 ? 3543 HOH B O     1 
HETATM 10530 O  O     . HOH HA 6 .   ? 39.779  29.727  141.203 1.00 44.78 ? 3544 HOH B O     1 
HETATM 10531 O  O     . HOH HA 6 .   ? 36.935  55.962  150.697 1.00 59.21 ? 3545 HOH B O     1 
HETATM 10532 O  O     . HOH HA 6 .   ? 46.859  64.207  143.914 1.00 52.04 ? 3546 HOH B O     1 
HETATM 10533 O  O     . HOH HA 6 .   ? 59.895  56.165  123.024 1.00 58.53 ? 3547 HOH B O     1 
HETATM 10534 O  O     . HOH HA 6 .   ? 53.480  66.724  141.026 1.00 36.44 ? 3548 HOH B O     1 
HETATM 10535 O  O     . HOH HA 6 .   ? 24.452  45.202  132.386 1.00 46.67 ? 3549 HOH B O     1 
HETATM 10536 O  O     . HOH HA 6 .   ? 19.350  67.103  130.418 1.00 42.79 ? 3550 HOH B O     1 
HETATM 10537 O  O     . HOH HA 6 .   ? 21.646  64.318  116.175 1.00 36.51 ? 3551 HOH B O     1 
HETATM 10538 O  O     . HOH HA 6 .   ? 27.290  74.870  114.594 1.00 52.35 ? 3552 HOH B O     1 
HETATM 10539 O  O     . HOH HA 6 .   ? 25.992  66.353  110.265 1.00 44.90 ? 3553 HOH B O     1 
HETATM 10540 O  O     . HOH HA 6 .   ? 29.762  69.939  106.023 1.00 39.57 ? 3554 HOH B O     1 
HETATM 10541 O  O     . HOH HA 6 .   ? 22.182  51.586  114.036 1.00 42.19 ? 3555 HOH B O     1 
HETATM 10542 O  O     . HOH HA 6 .   ? 37.067  58.402  139.261 1.00 35.87 ? 3556 HOH B O     1 
HETATM 10543 O  O     . HOH HA 6 .   ? 39.790  59.260  140.113 1.00 36.93 ? 3557 HOH B O     1 
HETATM 10544 O  O     . HOH HA 6 .   ? 26.577  42.746  137.870 1.00 51.35 ? 3558 HOH B O     1 
HETATM 10545 O  O     . HOH HA 6 .   ? 34.533  34.476  145.690 1.00 50.13 ? 3559 HOH B O     1 
HETATM 10546 O  O     . HOH HA 6 .   ? 55.205  54.731  157.338 1.00 56.62 ? 3560 HOH B O     1 
HETATM 10547 O  O     . HOH HA 6 .   ? 53.136  63.267  152.279 1.00 53.98 ? 3561 HOH B O     1 
HETATM 10548 O  O     . HOH HA 6 .   ? 24.531  59.953  136.660 1.00 50.88 ? 3562 HOH B O     1 
HETATM 10549 O  O     . HOH HA 6 .   ? 37.302  20.856  139.838 1.00 55.99 ? 3563 HOH B O     1 
HETATM 10550 O  O     . HOH HA 6 .   ? 56.291  59.194  140.799 1.00 52.89 ? 3564 HOH B O     1 
HETATM 10551 O  O     . HOH HA 6 .   ? 39.075  67.610  113.039 1.00 45.65 ? 3565 HOH B O     1 
HETATM 10552 O  O     . HOH HA 6 .   ? 32.037  62.636  99.331  1.00 54.77 ? 3566 HOH B O     1 
HETATM 10553 O  O     . HOH HA 6 .   ? 28.497  57.908  101.272 1.00 46.58 ? 3567 HOH B O     1 
HETATM 10554 O  O     . HOH HA 6 .   ? 42.395  68.270  103.948 1.00 59.41 ? 3568 HOH B O     1 
HETATM 10555 O  O     . HOH HA 6 .   ? 31.707  49.803  110.952 1.00 52.16 ? 3569 HOH B O     1 
HETATM 10556 O  O     . HOH HA 6 .   ? 25.487  75.703  120.318 1.00 53.36 ? 3570 HOH B O     1 
HETATM 10557 O  O     . HOH HA 6 .   ? 15.717  75.811  116.942 1.00 50.09 ? 3571 HOH B O     1 
HETATM 10558 O  O     . HOH HA 6 .   ? 41.150  34.328  152.528 1.00 48.90 ? 3572 HOH B O     1 
HETATM 10559 O  O     . HOH HA 6 .   ? 51.737  33.631  155.165 1.00 52.43 ? 3573 HOH B O     1 
HETATM 10560 O  O     . HOH HA 6 .   ? 56.798  39.520  150.041 1.00 41.51 ? 3574 HOH B O     1 
HETATM 10561 O  O     . HOH HA 6 .   ? 39.088  63.667  102.488 1.00 60.04 ? 3575 HOH B O     1 
HETATM 10562 O  O     . HOH HA 6 .   ? 60.122  55.603  141.324 1.00 48.63 ? 3576 HOH B O     1 
HETATM 10563 O  O     . HOH HA 6 .   ? 27.625  50.456  112.604 1.00 55.94 ? 3577 HOH B O     1 
HETATM 10564 O  O     . HOH HA 6 .   ? 21.264  49.186  115.680 1.00 54.59 ? 3578 HOH B O     1 
HETATM 10565 O  O     . HOH HA 6 .   ? 19.298  39.132  121.143 1.00 58.06 ? 3579 HOH B O     1 
HETATM 10566 O  O     . HOH HA 6 .   ? 19.524  53.268  130.981 1.00 42.23 ? 3580 HOH B O     1 
HETATM 10567 O  O     . HOH HA 6 .   ? 19.454  58.156  133.529 1.00 47.71 ? 3581 HOH B O     1 
HETATM 10568 O  O     . HOH HA 6 .   ? 17.920  56.553  121.870 1.00 54.51 ? 3582 HOH B O     1 
HETATM 10569 O  O     . HOH HA 6 .   ? 25.697  57.752  135.992 1.00 47.11 ? 3583 HOH B O     1 
HETATM 10570 O  O     . HOH HA 6 .   ? 15.618  59.911  128.190 1.00 54.52 ? 3584 HOH B O     1 
HETATM 10571 O  O     . HOH HA 6 .   ? 22.699  62.757  134.411 1.00 54.75 ? 3585 HOH B O     1 
HETATM 10572 O  O     . HOH HA 6 .   ? 18.761  63.996  111.806 1.00 54.46 ? 3586 HOH B O     1 
HETATM 10573 O  O     . HOH HA 6 .   ? 16.407  70.414  117.114 1.00 54.17 ? 3587 HOH B O     1 
HETATM 10574 O  O     . HOH HA 6 .   ? 23.293  71.690  130.606 1.00 46.45 ? 3588 HOH B O     1 
HETATM 10575 O  O     . HOH HA 6 .   ? 17.620  58.938  122.016 1.00 42.09 ? 3589 HOH B O     1 
HETATM 10576 O  O     . HOH HA 6 .   ? 15.190  65.014  128.287 1.00 44.05 ? 3590 HOH B O     1 
HETATM 10577 O  O     . HOH HA 6 .   ? 30.999  49.503  138.899 1.00 45.28 ? 3591 HOH B O     1 
HETATM 10578 O  O     . HOH HA 6 .   ? 35.922  30.450  139.496 1.00 40.28 ? 3592 HOH B O     1 
HETATM 10579 O  O     . HOH HA 6 .   ? 41.123  59.301  142.155 1.00 54.01 ? 3593 HOH B O     1 
HETATM 10580 O  O     . HOH HA 6 .   ? 37.708  18.932  144.094 1.00 49.52 ? 3594 HOH B O     1 
HETATM 10581 O  O     . HOH HA 6 .   ? 44.317  47.275  151.501 1.00 44.71 ? 3595 HOH B O     1 
HETATM 10582 O  O     . HOH HA 6 .   ? 44.055  41.553  151.562 1.00 48.18 ? 3596 HOH B O     1 
HETATM 10583 O  O     . HOH HA 6 .   ? 16.662  57.041  116.041 1.00 51.92 ? 3597 HOH B O     1 
HETATM 10584 O  O     . HOH HA 6 .   ? 29.429  64.660  102.228 1.00 59.00 ? 3598 HOH B O     1 
HETATM 10585 O  O     . HOH HA 6 .   ? 28.704  71.119  108.421 1.00 55.40 ? 3599 HOH B O     1 
HETATM 10586 O  O     . HOH HA 6 .   ? 47.520  16.827  136.918 1.00 52.70 ? 3600 HOH B O     1 
HETATM 10587 O  O     . HOH HA 6 .   ? 62.112  27.797  155.913 1.00 48.62 ? 3601 HOH B O     1 
HETATM 10588 O  O     . HOH HA 6 .   ? 43.386  60.002  142.463 1.00 50.42 ? 3602 HOH B O     1 
HETATM 10589 O  O     . HOH HA 6 .   ? 66.727  68.146  148.607 1.00 53.69 ? 3603 HOH B O     1 
HETATM 10590 O  O     . HOH HA 6 .   ? 50.940  56.619  140.920 1.00 52.64 ? 3604 HOH B O     1 
HETATM 10591 O  O     . HOH HA 6 .   ? 42.396  64.554  129.484 1.00 57.31 ? 3605 HOH B O     1 
HETATM 10592 O  O     . HOH HA 6 .   ? 28.617  65.495  126.580 1.00 60.00 ? 3606 HOH B O     1 
HETATM 10593 O  O     . HOH IA 6 .   ? 67.734  50.291  122.365 1.00 41.04 ? 7778 HOH C O     1 
HETATM 10594 O  O     . HOH IA 6 .   ? 69.786  35.266  126.355 1.00 26.90 ? 7779 HOH C O     1 
HETATM 10595 O  O     . HOH IA 6 .   ? 67.476  37.345  127.389 1.00 26.89 ? 7780 HOH C O     1 
HETATM 10596 O  O     . HOH IA 6 .   ? 70.874  32.969  131.285 1.00 17.61 ? 7781 HOH C O     1 
HETATM 10597 O  O     . HOH IA 6 .   ? 67.143  40.067  124.669 1.00 37.25 ? 7782 HOH C O     1 
HETATM 10598 O  O     . HOH IA 6 .   ? 67.295  30.821  126.333 1.00 23.61 ? 7783 HOH C O     1 
HETATM 10599 O  O     . HOH IA 6 .   ? 82.005  45.937  132.941 1.00 19.03 ? 7784 HOH C O     1 
HETATM 10600 O  O     . HOH IA 6 .   ? 64.675  45.875  140.385 1.00 19.02 ? 7785 HOH C O     1 
HETATM 10601 O  O     . HOH IA 6 .   ? 70.852  29.038  126.644 1.00 33.28 ? 7786 HOH C O     1 
HETATM 10602 O  O     . HOH IA 6 .   ? 61.157  19.968  137.325 1.00 34.11 ? 7787 HOH C O     1 
HETATM 10603 O  O     . HOH IA 6 .   ? 50.993  34.706  143.777 1.00 16.97 ? 7788 HOH C O     1 
HETATM 10604 O  O     . HOH IA 6 .   ? 63.103  42.904  142.383 1.00 17.51 ? 7789 HOH C O     1 
HETATM 10605 O  O     . HOH IA 6 .   ? 80.522  21.933  138.744 1.00 46.49 ? 7790 HOH C O     1 
HETATM 10606 O  O     . HOH IA 6 .   ? 40.696  39.393  117.689 1.00 34.18 ? 7791 HOH C O     1 
HETATM 10607 O  O     . HOH IA 6 .   ? 26.057  39.391  114.431 1.00 36.92 ? 7792 HOH C O     1 
HETATM 10608 O  O     . HOH IA 6 .   ? 52.286  44.271  118.068 1.00 30.23 ? 7793 HOH C O     1 
HETATM 10609 O  O     . HOH IA 6 .   ? 35.590  44.728  113.318 1.00 35.37 ? 7794 HOH C O     1 
HETATM 10610 O  O     . HOH IA 6 .   ? 57.051  49.867  119.802 1.00 31.24 ? 7795 HOH C O     1 
HETATM 10611 O  O     . HOH IA 6 .   ? 65.642  54.005  120.662 1.00 31.66 ? 7796 HOH C O     1 
HETATM 10612 O  O     . HOH IA 6 .   ? 63.327  36.648  120.964 1.00 34.62 ? 7797 HOH C O     1 
HETATM 10613 O  O     . HOH IA 6 .   ? 65.120  23.404  127.829 1.00 37.71 ? 7798 HOH C O     1 
HETATM 10614 O  O     . HOH IA 6 .   ? 78.597  48.117  139.418 1.00 26.94 ? 7799 HOH C O     1 
HETATM 10615 O  O     . HOH IA 6 .   ? 27.108  46.005  117.969 1.00 44.22 ? 7800 HOH C O     1 
HETATM 10616 O  O     . HOH IA 6 .   ? 52.982  24.109  129.984 1.00 32.78 ? 7801 HOH C O     1 
HETATM 10617 O  O     . HOH IA 6 .   ? 84.252  28.843  129.699 1.00 19.06 ? 7802 HOH C O     1 
HETATM 10618 O  O     . HOH IA 6 .   ? 27.908  43.747  117.061 1.00 59.84 ? 7803 HOH C O     1 
HETATM 10619 O  O     . HOH IA 6 .   ? 67.944  33.148  125.081 1.00 45.98 ? 7804 HOH C O     1 
HETATM 10620 O  O     . HOH IA 6 .   ? 44.535  29.934  126.560 1.00 22.72 ? 7805 HOH C O     1 
HETATM 10621 O  O     . HOH IA 6 .   ? 72.594  30.370  127.931 1.00 32.70 ? 7806 HOH C O     1 
HETATM 10622 O  O     . HOH IA 6 .   ? 49.182  40.955  127.519 1.00 26.19 ? 7807 HOH C O     1 
HETATM 10623 O  O     . HOH IA 6 .   ? 55.094  23.966  128.196 1.00 28.45 ? 7808 HOH C O     1 
HETATM 10624 O  O     . HOH IA 6 .   ? 75.206  29.893  128.248 1.00 21.86 ? 7809 HOH C O     1 
HETATM 10625 O  O     . HOH IA 6 .   ? 70.646  48.378  131.630 1.00 16.93 ? 7810 HOH C O     1 
HETATM 10626 O  O     . HOH IA 6 .   ? 30.576  31.482  128.437 1.00 29.20 ? 7811 HOH C O     1 
HETATM 10627 O  O     . HOH IA 6 .   ? 80.834  21.503  129.378 1.00 38.97 ? 7812 HOH C O     1 
HETATM 10628 O  O     . HOH IA 6 .   ? 68.112  49.013  124.711 1.00 37.91 ? 7813 HOH C O     1 
HETATM 10629 O  O     . HOH IA 6 .   ? 47.074  42.541  123.728 1.00 30.04 ? 7814 HOH C O     1 
HETATM 10630 O  O     . HOH IA 6 .   ? 47.342  42.262  126.338 1.00 24.50 ? 7815 HOH C O     1 
HETATM 10631 O  O     . HOH IA 6 .   ? 76.232  44.507  143.879 1.00 32.18 ? 7816 HOH C O     1 
HETATM 10632 O  O     . HOH IA 6 .   ? 29.845  33.128  130.874 1.00 27.62 ? 7817 HOH C O     1 
HETATM 10633 O  O     . HOH IA 6 .   ? 41.406  29.620  128.835 1.00 28.94 ? 7818 HOH C O     1 
HETATM 10634 O  O     . HOH IA 6 .   ? 70.105  32.730  127.098 1.00 27.02 ? 7819 HOH C O     1 
HETATM 10635 O  O     . HOH IA 6 .   ? 69.018  42.128  123.692 1.00 53.38 ? 7820 HOH C O     1 
HETATM 10636 O  O     . HOH IA 6 .   ? 43.536  32.608  133.134 1.00 18.40 ? 7821 HOH C O     1 
HETATM 10637 O  O     . HOH IA 6 .   ? 42.457  27.976  126.510 1.00 29.84 ? 7822 HOH C O     1 
HETATM 10638 O  O     . HOH IA 6 .   ? 64.797  39.482  128.903 1.00 46.25 ? 7823 HOH C O     1 
HETATM 10639 O  O     . HOH IA 6 .   ? 63.479  47.328  138.450 1.00 16.43 ? 7824 HOH C O     1 
HETATM 10640 O  O     . HOH IA 6 .   ? 76.589  17.725  142.328 1.00 54.89 ? 7825 HOH C O     1 
HETATM 10641 O  O     . HOH IA 6 .   ? 64.295  41.317  131.860 1.00 28.71 ? 7826 HOH C O     1 
HETATM 10642 O  O     . HOH IA 6 .   ? 49.242  37.135  135.332 1.00 22.98 ? 7827 HOH C O     1 
HETATM 10643 O  O     . HOH IA 6 .   ? 66.685  49.112  126.955 1.00 26.91 ? 7828 HOH C O     1 
HETATM 10644 O  O     . HOH IA 6 .   ? 65.865  37.104  129.851 1.00 24.05 ? 7829 HOH C O     1 
HETATM 10645 O  O     . HOH IA 6 .   ? 79.783  27.463  136.087 1.00 22.91 ? 7830 HOH C O     1 
HETATM 10646 O  O     . HOH IA 6 .   ? 52.587  19.330  136.581 1.00 28.32 ? 7831 HOH C O     1 
HETATM 10647 O  O     . HOH IA 6 .   ? 83.991  21.642  151.061 1.00 24.44 ? 7832 HOH C O     1 
HETATM 10648 O  O     . HOH IA 6 .   ? 63.322  21.465  137.686 1.00 26.77 ? 7833 HOH C O     1 
HETATM 10649 O  O     . HOH IA 6 .   ? 68.525  50.187  131.529 1.00 20.94 ? 7834 HOH C O     1 
HETATM 10650 O  O     . HOH IA 6 .   ? 62.956  39.131  132.626 1.00 16.61 ? 7835 HOH C O     1 
HETATM 10651 O  O     . HOH IA 6 .   ? 76.036  48.043  138.612 1.00 26.30 ? 7836 HOH C O     1 
HETATM 10652 O  O     . HOH IA 6 .   ? 67.516  50.741  134.047 1.00 23.94 ? 7837 HOH C O     1 
HETATM 10653 O  O     . HOH IA 6 .   ? 60.499  20.676  139.684 1.00 28.03 ? 7838 HOH C O     1 
HETATM 10654 O  O     . HOH IA 6 .   ? 83.865  29.399  132.579 1.00 18.87 ? 7839 HOH C O     1 
HETATM 10655 O  O     . HOH IA 6 .   ? 83.833  27.966  135.076 1.00 23.58 ? 7840 HOH C O     1 
HETATM 10656 O  O     . HOH IA 6 .   ? 88.425  27.497  142.400 1.00 31.52 ? 7841 HOH C O     1 
HETATM 10657 O  O     . HOH IA 6 .   ? 83.297  25.076  141.845 1.00 19.27 ? 7842 HOH C O     1 
HETATM 10658 O  O     . HOH IA 6 .   ? 82.161  22.512  141.082 1.00 23.36 ? 7843 HOH C O     1 
HETATM 10659 O  O     . HOH IA 6 .   ? 78.769  25.021  137.534 1.00 24.04 ? 7844 HOH C O     1 
HETATM 10660 O  O     . HOH IA 6 .   ? 74.129  23.002  129.460 1.00 28.20 ? 7845 HOH C O     1 
HETATM 10661 O  O     . HOH IA 6 .   ? 86.414  33.912  141.296 1.00 23.17 ? 7846 HOH C O     1 
HETATM 10662 O  O     . HOH IA 6 .   ? 86.982  23.989  139.292 1.00 34.41 ? 7847 HOH C O     1 
HETATM 10663 O  O     . HOH IA 6 .   ? 87.709  25.439  137.217 1.00 45.56 ? 7848 HOH C O     1 
HETATM 10664 O  O     . HOH IA 6 .   ? 88.559  33.174  142.495 1.00 34.98 ? 7849 HOH C O     1 
HETATM 10665 O  O     . HOH IA 6 .   ? 82.374  27.484  148.789 1.00 19.81 ? 7850 HOH C O     1 
HETATM 10666 O  O     . HOH IA 6 .   ? 83.969  24.401  151.235 1.00 21.16 ? 7851 HOH C O     1 
HETATM 10667 O  O     . HOH IA 6 .   ? 89.578  26.195  150.323 1.00 22.96 ? 7852 HOH C O     1 
HETATM 10668 O  O     . HOH IA 6 .   ? 75.307  27.208  147.058 1.00 18.94 ? 7853 HOH C O     1 
HETATM 10669 O  O     . HOH IA 6 .   ? 67.017  22.219  151.575 1.00 28.48 ? 7854 HOH C O     1 
HETATM 10670 O  O     . HOH IA 6 .   ? 66.092  21.056  148.691 1.00 31.05 ? 7855 HOH C O     1 
HETATM 10671 O  O     . HOH IA 6 .   ? 63.726  22.255  148.584 1.00 36.39 ? 7856 HOH C O     1 
HETATM 10672 O  O     . HOH IA 6 .   ? 63.213  14.816  144.964 1.00 53.28 ? 7857 HOH C O     1 
HETATM 10673 O  O     . HOH IA 6 .   ? 61.681  23.501  151.047 1.00 37.07 ? 7858 HOH C O     1 
HETATM 10674 O  O     . HOH IA 6 .   ? 56.451  22.439  152.783 1.00 25.77 ? 7859 HOH C O     1 
HETATM 10675 O  O     . HOH IA 6 .   ? 60.702  15.623  145.548 1.00 30.97 ? 7860 HOH C O     1 
HETATM 10676 O  O     . HOH IA 6 .   ? 43.658  39.004  112.202 1.00 57.41 ? 7861 HOH C O     1 
HETATM 10677 O  O     . HOH IA 6 .   ? 56.077  39.045  140.655 1.00 19.04 ? 7862 HOH C O     1 
HETATM 10678 O  O     . HOH IA 6 .   ? 55.654  39.996  143.131 1.00 20.18 ? 7863 HOH C O     1 
HETATM 10679 O  O     . HOH IA 6 .   ? 53.197  38.455  140.187 1.00 29.13 ? 7864 HOH C O     1 
HETATM 10680 O  O     . HOH IA 6 .   ? 55.663  39.360  137.938 1.00 18.31 ? 7865 HOH C O     1 
HETATM 10681 O  O     . HOH IA 6 .   ? 57.005  42.042  144.486 1.00 22.39 ? 7866 HOH C O     1 
HETATM 10682 O  O     . HOH IA 6 .   ? 46.111  40.557  137.585 1.00 20.49 ? 7867 HOH C O     1 
HETATM 10683 O  O     . HOH IA 6 .   ? 54.773  42.962  146.050 1.00 30.15 ? 7868 HOH C O     1 
HETATM 10684 O  O     . HOH IA 6 .   ? 59.476  39.425  149.165 1.00 20.55 ? 7869 HOH C O     1 
HETATM 10685 O  O     . HOH IA 6 .   ? 52.742  25.028  132.462 1.00 30.68 ? 7870 HOH C O     1 
HETATM 10686 O  O     . HOH IA 6 .   ? 47.945  27.389  134.984 1.00 26.13 ? 7871 HOH C O     1 
HETATM 10687 O  O     . HOH IA 6 .   ? 48.242  24.621  129.760 1.00 37.11 ? 7872 HOH C O     1 
HETATM 10688 O  O     . HOH IA 6 .   ? 60.829  23.485  129.855 1.00 50.13 ? 7873 HOH C O     1 
HETATM 10689 O  O     . HOH IA 6 .   ? 49.914  38.527  128.616 1.00 20.05 ? 7874 HOH C O     1 
HETATM 10690 O  O     . HOH IA 6 .   ? 62.099  24.460  127.958 1.00 52.03 ? 7875 HOH C O     1 
HETATM 10691 O  O     . HOH IA 6 .   ? 78.820  34.064  142.475 1.00 19.68 ? 7876 HOH C O     1 
HETATM 10692 O  O     . HOH IA 6 .   ? 79.265  35.527  144.634 1.00 17.03 ? 7877 HOH C O     1 
HETATM 10693 O  O     . HOH IA 6 .   ? 59.464  53.478  131.736 1.00 37.35 ? 7878 HOH C O     1 
HETATM 10694 O  O     . HOH IA 6 .   ? 60.467  52.264  134.372 1.00 34.52 ? 7879 HOH C O     1 
HETATM 10695 O  O     . HOH IA 6 .   ? 23.616  32.641  126.396 1.00 40.23 ? 7880 HOH C O     1 
HETATM 10696 O  O     . HOH IA 6 .   ? 27.879  34.646  134.133 1.00 50.26 ? 7881 HOH C O     1 
HETATM 10697 O  O     . HOH IA 6 .   ? 27.266  31.658  134.653 1.00 48.64 ? 7882 HOH C O     1 
HETATM 10698 O  O     . HOH IA 6 .   ? 41.761  22.167  137.031 1.00 44.58 ? 7883 HOH C O     1 
HETATM 10699 O  O     . HOH IA 6 .   ? 42.322  25.859  128.638 1.00 46.64 ? 7884 HOH C O     1 
HETATM 10700 O  O     . HOH IA 6 .   ? 43.936  22.481  139.305 1.00 41.16 ? 7885 HOH C O     1 
HETATM 10701 O  O     . HOH IA 6 .   ? 89.619  28.902  150.860 1.00 37.42 ? 7886 HOH C O     1 
HETATM 10702 O  O     . HOH IA 6 .   ? 62.586  32.850  153.977 1.00 36.88 ? 7887 HOH C O     1 
HETATM 10703 O  O     . HOH IA 6 .   ? 53.996  28.887  143.880 1.00 34.68 ? 7888 HOH C O     1 
HETATM 10704 O  O     . HOH IA 6 .   ? 57.706  40.067  152.902 1.00 41.95 ? 7889 HOH C O     1 
HETATM 10705 O  O     . HOH IA 6 .   ? 59.187  39.158  155.446 1.00 56.05 ? 7890 HOH C O     1 
HETATM 10706 O  O     . HOH IA 6 .   ? 62.009  45.976  156.838 1.00 57.63 ? 7891 HOH C O     1 
HETATM 10707 O  O     . HOH IA 6 .   ? 58.790  31.639  150.021 1.00 17.44 ? 7892 HOH C O     1 
HETATM 10708 O  O     . HOH IA 6 .   ? 65.098  50.933  139.241 1.00 40.06 ? 7893 HOH C O     1 
HETATM 10709 O  O     . HOH IA 6 .   ? 60.098  52.431  121.761 1.00 50.37 ? 7894 HOH C O     1 
HETATM 10710 O  O     . HOH IA 6 .   ? 43.200  41.959  117.848 1.00 49.77 ? 7895 HOH C O     1 
HETATM 10711 O  O     . HOH IA 6 .   ? 31.992  44.836  113.844 1.00 44.96 ? 7896 HOH C O     1 
HETATM 10712 O  O     . HOH IA 6 .   ? 39.596  46.401  110.979 1.00 58.28 ? 7897 HOH C O     1 
HETATM 10713 O  O     . HOH IA 6 .   ? 48.918  42.509  122.277 1.00 41.01 ? 7898 HOH C O     1 
HETATM 10714 O  O     . HOH IA 6 .   ? 58.665  13.978  145.011 1.00 40.98 ? 7899 HOH C O     1 
HETATM 10715 O  O     . HOH IA 6 .   ? 60.265  15.029  148.339 1.00 48.15 ? 7900 HOH C O     1 
HETATM 10716 O  O     . HOH IA 6 .   ? 88.076  30.651  151.747 1.00 47.99 ? 7901 HOH C O     1 
HETATM 10717 O  O     . HOH IA 6 .   ? 48.995  14.579  149.382 1.00 52.45 ? 7902 HOH C O     1 
HETATM 10718 O  O     . HOH IA 6 .   ? 65.331  15.438  140.230 1.00 35.67 ? 7903 HOH C O     1 
HETATM 10719 O  O     . HOH IA 6 .   ? 58.344  20.222  133.341 1.00 35.01 ? 7904 HOH C O     1 
HETATM 10720 O  O     . HOH IA 6 .   ? 62.084  24.691  125.684 1.00 50.26 ? 7905 HOH C O     1 
HETATM 10721 O  O     . HOH IA 6 .   ? 67.682  14.751  139.036 1.00 37.65 ? 7906 HOH C O     1 
HETATM 10722 O  O     . HOH IA 6 .   ? 68.458  14.816  136.377 1.00 44.57 ? 7907 HOH C O     1 
HETATM 10723 O  O     . HOH IA 6 .   ? 70.224  17.375  135.837 1.00 36.82 ? 7908 HOH C O     1 
HETATM 10724 O  O     . HOH IA 6 .   ? 76.110  17.170  144.640 1.00 44.76 ? 7909 HOH C O     1 
HETATM 10725 O  O     . HOH IA 6 .   ? 76.031  14.707  141.145 1.00 43.15 ? 7910 HOH C O     1 
HETATM 10726 O  O     . HOH IA 6 .   ? 79.715  17.000  133.905 1.00 54.60 ? 7911 HOH C O     1 
HETATM 10727 O  O     . HOH IA 6 .   ? 79.186  19.471  146.837 1.00 29.32 ? 7912 HOH C O     1 
HETATM 10728 O  O     . HOH IA 6 .   ? 86.935  17.709  141.368 1.00 47.89 ? 7913 HOH C O     1 
HETATM 10729 O  O     . HOH IA 6 .   ? 89.443  14.780  145.577 1.00 41.93 ? 7914 HOH C O     1 
HETATM 10730 O  O     . HOH IA 6 .   ? 87.734  17.073  145.784 1.00 39.75 ? 7915 HOH C O     1 
HETATM 10731 O  O     . HOH IA 6 .   ? 79.530  28.215  155.781 1.00 40.56 ? 7916 HOH C O     1 
HETATM 10732 O  O     . HOH IA 6 .   ? 76.270  40.236  150.719 1.00 21.07 ? 7917 HOH C O     1 
HETATM 10733 O  O     . HOH IA 6 .   ? 78.675  39.963  150.011 1.00 44.28 ? 7918 HOH C O     1 
HETATM 10734 O  O     . HOH IA 6 .   ? 76.091  42.704  152.292 1.00 36.60 ? 7919 HOH C O     1 
HETATM 10735 O  O     . HOH IA 6 .   ? 68.523  21.063  155.109 1.00 44.18 ? 7920 HOH C O     1 
HETATM 10736 O  O     . HOH IA 6 .   ? 81.950  12.973  144.463 1.00 43.79 ? 7921 HOH C O     1 
HETATM 10737 O  O     . HOH IA 6 .   ? 47.775  25.174  134.089 1.00 36.97 ? 7922 HOH C O     1 
HETATM 10738 O  O     . HOH IA 6 .   ? 47.000  22.076  133.305 1.00 46.02 ? 7923 HOH C O     1 
HETATM 10739 O  O     . HOH IA 6 .   ? 39.952  27.265  122.780 1.00 37.87 ? 7924 HOH C O     1 
HETATM 10740 O  O     . HOH IA 6 .   ? 47.524  30.504  119.762 1.00 37.05 ? 7925 HOH C O     1 
HETATM 10741 O  O     . HOH IA 6 .   ? 56.036  39.065  113.786 1.00 34.42 ? 7926 HOH C O     1 
HETATM 10742 O  O     . HOH IA 6 .   ? 66.280  44.025  124.716 1.00 31.93 ? 7927 HOH C O     1 
HETATM 10743 O  O     . HOH IA 6 .   ? 68.643  44.911  126.140 1.00 26.73 ? 7928 HOH C O     1 
HETATM 10744 O  O     . HOH IA 6 .   ? 66.011  49.490  120.631 1.00 54.33 ? 7929 HOH C O     1 
HETATM 10745 O  O     . HOH IA 6 .   ? 70.377  42.895  126.724 1.00 33.18 ? 7930 HOH C O     1 
HETATM 10746 O  O     . HOH IA 6 .   ? 61.486  50.718  118.372 1.00 59.48 ? 7931 HOH C O     1 
HETATM 10747 O  O     . HOH IA 6 .   ? 36.687  30.630  117.147 1.00 42.95 ? 7932 HOH C O     1 
HETATM 10748 O  O     . HOH IA 6 .   ? 37.518  33.462  119.646 1.00 38.67 ? 7933 HOH C O     1 
HETATM 10749 O  O     . HOH IA 6 .   ? 37.582  33.410  117.081 1.00 50.42 ? 7934 HOH C O     1 
HETATM 10750 O  O     . HOH IA 6 .   ? 34.761  24.397  125.000 1.00 53.83 ? 7935 HOH C O     1 
HETATM 10751 O  O     . HOH IA 6 .   ? 29.617  44.698  114.401 1.00 59.50 ? 7936 HOH C O     1 
HETATM 10752 O  O     . HOH IA 6 .   ? 26.324  24.742  125.636 1.00 53.69 ? 7937 HOH C O     1 
HETATM 10753 O  O     . HOH IA 6 .   ? 28.683  27.673  122.007 1.00 53.96 ? 7938 HOH C O     1 
HETATM 10754 O  O     . HOH IA 6 .   ? 30.617  26.039  123.415 1.00 43.88 ? 7939 HOH C O     1 
HETATM 10755 O  O     . HOH IA 6 .   ? 27.311  25.052  129.402 1.00 60.04 ? 7940 HOH C O     1 
HETATM 10756 O  O     . HOH IA 6 .   ? 25.516  26.920  130.583 1.00 50.85 ? 7941 HOH C O     1 
HETATM 10757 O  O     . HOH IA 6 .   ? 23.699  29.505  128.273 1.00 54.58 ? 7942 HOH C O     1 
HETATM 10758 O  O     . HOH IA 6 .   ? 24.960  35.969  116.206 1.00 53.99 ? 7943 HOH C O     1 
HETATM 10759 O  O     . HOH IA 6 .   ? 32.063  42.976  111.672 1.00 55.46 ? 7944 HOH C O     1 
HETATM 10760 O  O     . HOH IA 6 .   ? 64.116  50.599  125.795 1.00 40.93 ? 7945 HOH C O     1 
HETATM 10761 O  O     . HOH IA 6 .   ? 62.241  52.749  119.821 1.00 50.16 ? 7946 HOH C O     1 
HETATM 10762 O  O     . HOH IA 6 .   ? 66.978  45.182  157.263 1.00 35.80 ? 7947 HOH C O     1 
HETATM 10763 O  O     . HOH IA 6 .   ? 73.453  46.171  154.379 1.00 37.15 ? 7948 HOH C O     1 
HETATM 10764 O  O     . HOH IA 6 .   ? 72.975  47.430  147.596 1.00 45.57 ? 7949 HOH C O     1 
HETATM 10765 O  O     . HOH IA 6 .   ? 64.932  29.947  156.492 1.00 35.66 ? 7950 HOH C O     1 
HETATM 10766 O  O     . HOH IA 6 .   ? 61.823  35.056  157.820 1.00 45.68 ? 7951 HOH C O     1 
HETATM 10767 O  O     . HOH IA 6 .   ? 70.570  29.613  161.383 1.00 41.40 ? 7952 HOH C O     1 
HETATM 10768 O  O     . HOH IA 6 .   ? 82.212  35.687  163.592 1.00 56.35 ? 7953 HOH C O     1 
HETATM 10769 O  O     . HOH IA 6 .   ? 81.077  33.834  160.361 1.00 46.15 ? 7954 HOH C O     1 
HETATM 10770 O  O     . HOH IA 6 .   ? 82.694  35.892  160.686 1.00 40.80 ? 7955 HOH C O     1 
HETATM 10771 O  O     . HOH IA 6 .   ? 80.219  31.919  162.286 1.00 48.55 ? 7956 HOH C O     1 
HETATM 10772 O  O     . HOH IA 6 .   ? 61.717  40.284  158.962 1.00 51.94 ? 7957 HOH C O     1 
HETATM 10773 O  O     . HOH IA 6 .   ? 64.166  44.964  157.029 1.00 43.02 ? 7958 HOH C O     1 
HETATM 10774 O  O     . HOH IA 6 .   ? 84.720  21.493  133.865 1.00 52.80 ? 7959 HOH C O     1 
HETATM 10775 O  O     . HOH IA 6 .   ? 89.033  34.256  149.853 1.00 44.94 ? 7960 HOH C O     1 
HETATM 10776 O  O     . HOH IA 6 .   ? 73.669  27.506  119.115 1.00 60.04 ? 7961 HOH C O     1 
HETATM 10777 O  O     . HOH IA 6 .   ? 65.028  20.577  152.239 1.00 49.79 ? 7962 HOH C O     1 
HETATM 10778 O  O     . HOH IA 6 .   ? 67.805  11.530  141.337 1.00 49.72 ? 7963 HOH C O     1 
HETATM 10779 O  O     . HOH IA 6 .   ? 85.240  27.177  141.463 1.00 45.41 ? 7964 HOH C O     1 
HETATM 10780 O  O     . HOH IA 6 .   ? 86.087  32.237  156.538 1.00 42.17 ? 7965 HOH C O     1 
HETATM 10781 O  O     . HOH IA 6 .   ? 83.010  19.348  151.668 1.00 39.86 ? 7966 HOH C O     1 
HETATM 10782 O  O     . HOH IA 6 .   ? 70.343  22.993  124.958 1.00 52.10 ? 7967 HOH C O     1 
HETATM 10783 O  O     . HOH IA 6 .   ? 65.899  17.490  133.506 1.00 46.85 ? 7968 HOH C O     1 
HETATM 10784 O  O     . HOH IA 6 .   ? 58.140  15.121  138.505 1.00 56.14 ? 7969 HOH C O     1 
HETATM 10785 O  O     . HOH IA 6 .   ? 42.873  27.452  123.866 1.00 43.99 ? 7970 HOH C O     1 
HETATM 10786 O  O     . HOH IA 6 .   ? 63.236  25.171  123.460 1.00 54.59 ? 7971 HOH C O     1 
HETATM 10787 O  O     . HOH IA 6 .   ? 55.297  43.030  111.953 1.00 41.04 ? 7972 HOH C O     1 
HETATM 10788 O  O     . HOH IA 6 .   ? 26.575  29.604  123.049 1.00 53.02 ? 7973 HOH C O     1 
HETATM 10789 O  O     . HOH IA 6 .   ? 34.752  27.621  118.452 1.00 42.44 ? 7974 HOH C O     1 
HETATM 10790 O  O     . HOH IA 6 .   ? 36.162  34.084  115.174 1.00 50.26 ? 7975 HOH C O     1 
HETATM 10791 O  O     . HOH IA 6 .   ? 37.134  37.527  115.949 1.00 49.83 ? 7976 HOH C O     1 
HETATM 10792 O  O     . HOH IA 6 .   ? 28.612  46.756  113.449 1.00 44.86 ? 7977 HOH C O     1 
HETATM 10793 O  O     . HOH IA 6 .   ? 27.599  38.101  110.392 1.00 45.62 ? 7978 HOH C O     1 
HETATM 10794 O  O     . HOH IA 6 .   ? 66.576  43.633  159.493 1.00 43.91 ? 7979 HOH C O     1 
HETATM 10795 O  O     . HOH IA 6 .   ? 26.400  30.355  137.020 1.00 56.42 ? 7980 HOH C O     1 
HETATM 10796 O  O     . HOH IA 6 .   ? 51.838  15.233  140.388 1.00 53.78 ? 7981 HOH C O     1 
HETATM 10797 O  O     . HOH IA 6 .   ? 54.938  16.041  141.574 1.00 58.85 ? 7982 HOH C O     1 
HETATM 10798 O  O     . HOH IA 6 .   ? 71.595  19.115  133.173 1.00 46.96 ? 7983 HOH C O     1 
HETATM 10799 O  O     . HOH IA 6 .   ? 70.285  14.154  143.863 1.00 48.54 ? 7984 HOH C O     1 
HETATM 10800 O  O     . HOH IA 6 .   ? 63.943  14.289  138.174 1.00 45.15 ? 7985 HOH C O     1 
HETATM 10801 O  O     . HOH IA 6 .   ? 74.752  15.361  146.386 1.00 46.56 ? 7986 HOH C O     1 
HETATM 10802 O  O     . HOH IA 6 .   ? 87.591  32.301  149.970 1.00 46.74 ? 7987 HOH C O     1 
HETATM 10803 O  O     . HOH IA 6 .   ? 89.712  38.342  147.451 1.00 35.02 ? 7988 HOH C O     1 
HETATM 10804 O  O     . HOH IA 6 .   ? 47.883  31.762  117.495 1.00 43.62 ? 7989 HOH C O     1 
HETATM 10805 O  O     . HOH IA 6 .   ? 26.032  28.592  125.127 1.00 60.04 ? 7990 HOH C O     1 
HETATM 10806 O  O     . HOH IA 6 .   ? 57.695  46.528  151.647 1.00 52.29 ? 7991 HOH C O     1 
HETATM 10807 O  O     . HOH IA 6 .   ? 51.384  14.249  149.306 1.00 56.31 ? 7992 HOH C O     1 
HETATM 10808 O  O     . HOH IA 6 .   ? 44.970  15.683  151.479 1.00 59.86 ? 7993 HOH C O     1 
HETATM 10809 O  O     . HOH IA 6 .   ? 54.821  17.989  155.274 1.00 51.70 ? 7994 HOH C O     1 
HETATM 10810 O  O     . HOH IA 6 .   ? 46.381  21.037  136.974 1.00 40.16 ? 7995 HOH C O     1 
HETATM 10811 O  O     . HOH IA 6 .   ? 75.563  18.524  132.879 1.00 53.64 ? 7996 HOH C O     1 
HETATM 10812 O  O     . HOH IA 6 .   ? 85.446  17.145  137.609 1.00 39.37 ? 7997 HOH C O     1 
HETATM 10813 O  O     . HOH IA 6 .   ? 77.986  41.236  152.208 1.00 60.02 ? 7998 HOH C O     1 
HETATM 10814 O  O     . HOH IA 6 .   ? 81.727  38.499  160.163 1.00 37.53 ? 7999 HOH C O     1 
HETATM 10815 O  O     . HOH IA 6 .   ? 85.261  28.376  155.750 1.00 40.57 ? 8000 HOH C O     1 
HETATM 10816 O  O     . HOH IA 6 .   ? 44.253  25.421  122.865 1.00 46.78 ? 8001 HOH C O     1 
HETATM 10817 O  O     . HOH IA 6 .   ? 50.005  25.033  132.436 1.00 38.10 ? 8002 HOH C O     1 
HETATM 10818 O  O     . HOH IA 6 .   ? 55.945  41.927  109.451 1.00 50.98 ? 8003 HOH C O     1 
HETATM 10819 O  O     . HOH IA 6 .   ? 29.898  29.357  120.409 1.00 53.24 ? 8004 HOH C O     1 
HETATM 10820 O  O     . HOH IA 6 .   ? 45.345  40.739  118.544 1.00 59.41 ? 8005 HOH C O     1 
HETATM 10821 O  O     . HOH IA 6 .   ? 69.970  46.904  125.039 1.00 27.17 ? 8006 HOH C O     1 
HETATM 10822 O  O     . HOH IA 6 .   ? 70.580  47.348  111.753 1.00 54.10 ? 8007 HOH C O     1 
HETATM 10823 O  O     . HOH IA 6 .   ? 71.299  44.895  162.148 1.00 51.24 ? 8008 HOH C O     1 
HETATM 10824 O  O     . HOH IA 6 .   ? 66.890  23.569  155.411 1.00 45.67 ? 8009 HOH C O     1 
HETATM 10825 O  O     . HOH IA 6 .   ? 68.191  47.193  158.275 1.00 45.65 ? 8010 HOH C O     1 
HETATM 10826 O  O     . HOH IA 6 .   ? 62.385  46.627  153.136 1.00 32.78 ? 8011 HOH C O     1 
HETATM 10827 O  O     . HOH IA 6 .   ? 77.849  20.528  150.230 1.00 32.20 ? 8012 HOH C O     1 
HETATM 10828 O  O     . HOH IA 6 .   ? 79.006  25.788  156.623 1.00 57.77 ? 8013 HOH C O     1 
HETATM 10829 O  O     . HOH IA 6 .   ? 81.520  28.008  157.394 1.00 51.33 ? 8014 HOH C O     1 
HETATM 10830 O  O     . HOH IA 6 .   ? 76.320  17.427  152.557 1.00 45.35 ? 8015 HOH C O     1 
HETATM 10831 O  O     . HOH IA 6 .   ? 68.967  23.321  127.049 1.00 40.42 ? 8016 HOH C O     1 
HETATM 10832 O  O     . HOH IA 6 .   ? 73.941  39.134  133.661 1.00 43.56 ? 8017 HOH C O     1 
HETATM 10833 O  O     . HOH IA 6 .   ? 66.017  29.630  159.328 1.00 50.29 ? 8018 HOH C O     1 
HETATM 10834 O  O     . HOH IA 6 .   ? 89.903  23.139  142.043 1.00 35.96 ? 8019 HOH C O     1 
HETATM 10835 O  O     . HOH IA 6 .   ? 88.703  30.047  143.186 1.00 43.62 ? 8020 HOH C O     1 
HETATM 10836 O  O     . HOH IA 6 .   ? 80.958  39.672  149.611 1.00 50.99 ? 8021 HOH C O     1 
HETATM 10837 O  O     . HOH IA 6 .   ? 66.993  52.724  108.181 1.00 31.77 ? 8022 HOH C O     1 
HETATM 10838 O  O     . HOH IA 6 .   ? 64.360  53.696  106.695 1.00 42.27 ? 8023 HOH C O     1 
HETATM 10839 O  O     . HOH IA 6 .   ? 67.824  56.224  107.564 1.00 40.21 ? 8024 HOH C O     1 
HETATM 10840 O  O     . HOH IA 6 .   ? 66.417  54.712  106.727 1.00 34.74 ? 8025 HOH C O     1 
HETATM 10841 O  O     . HOH IA 6 .   ? 71.956  55.816  109.419 1.00 36.60 ? 8026 HOH C O     1 
HETATM 10842 O  O     . HOH IA 6 .   ? 70.149  53.641  117.434 1.00 43.52 ? 8027 HOH C O     1 
HETATM 10843 O  O     . HOH IA 6 .   ? 69.114  48.794  120.360 1.00 40.84 ? 8028 HOH C O     1 
HETATM 10844 O  O     . HOH IA 6 .   ? 80.635  36.915  161.567 1.00 47.65 ? 8029 HOH C O     1 
HETATM 10845 O  O     . HOH JA 6 .   ? 94.545  40.312  116.449 1.00 17.30 ? 1000 HOH D O     1 
HETATM 10846 O  O     . HOH JA 6 .   ? 96.755  56.036  113.121 1.00 20.83 ? 1001 HOH D O     1 
HETATM 10847 O  O     . HOH JA 6 .   ? 85.861  62.337  113.461 1.00 15.26 ? 1002 HOH D O     1 
HETATM 10848 O  O     . HOH JA 6 .   ? 78.150  60.215  113.945 1.00 17.08 ? 1003 HOH D O     1 
HETATM 10849 O  O     . HOH JA 6 .   ? 75.115  56.294  120.730 1.00 17.39 ? 1004 HOH D O     1 
HETATM 10850 O  O     . HOH JA 6 .   ? 74.969  62.284  118.167 1.00 21.54 ? 1005 HOH D O     1 
HETATM 10851 O  O     . HOH JA 6 .   ? 101.979 45.004  118.457 1.00 21.52 ? 1006 HOH D O     1 
HETATM 10852 O  O     . HOH JA 6 .   ? 83.720  35.548  119.982 1.00 30.69 ? 1007 HOH D O     1 
HETATM 10853 O  O     . HOH JA 6 .   ? 85.627  41.809  119.939 1.00 14.12 ? 1008 HOH D O     1 
HETATM 10854 O  O     . HOH JA 6 .   ? 67.379  52.816  123.664 1.00 41.14 ? 1009 HOH D O     1 
HETATM 10855 O  O     . HOH JA 6 .   ? 95.709  60.631  126.700 1.00 21.64 ? 1010 HOH D O     1 
HETATM 10856 O  O     . HOH JA 6 .   ? 96.805  40.119  123.387 1.00 18.94 ? 1011 HOH D O     1 
HETATM 10857 O  O     . HOH JA 6 .   ? 102.695 36.974  124.313 1.00 29.32 ? 1012 HOH D O     1 
HETATM 10858 O  O     . HOH JA 6 .   ? 73.827  73.693  124.182 1.00 20.45 ? 1013 HOH D O     1 
HETATM 10859 O  O     . HOH JA 6 .   ? 70.573  55.207  124.363 1.00 15.41 ? 1014 HOH D O     1 
HETATM 10860 O  O     . HOH JA 6 .   ? 86.802  74.656  127.825 1.00 26.19 ? 1015 HOH D O     1 
HETATM 10861 O  O     . HOH JA 6 .   ? 103.284 57.462  125.919 1.00 26.18 ? 1016 HOH D O     1 
HETATM 10862 O  O     . HOH JA 6 .   ? 78.153  57.786  130.625 1.00 17.52 ? 1017 HOH D O     1 
HETATM 10863 O  O     . HOH JA 6 .   ? 77.277  72.297  131.744 1.00 24.82 ? 1018 HOH D O     1 
HETATM 10864 O  O     . HOH JA 6 .   ? 93.061  43.447  128.767 1.00 19.44 ? 1019 HOH D O     1 
HETATM 10865 O  O     . HOH JA 6 .   ? 80.386  55.471  133.668 1.00 23.95 ? 1020 HOH D O     1 
HETATM 10866 O  O     . HOH JA 6 .   ? 80.679  78.031  129.076 1.00 17.95 ? 1021 HOH D O     1 
HETATM 10867 O  O     . HOH JA 6 .   ? 85.639  51.322  132.729 1.00 16.31 ? 1022 HOH D O     1 
HETATM 10868 O  O     . HOH JA 6 .   ? 78.907  91.373  132.423 1.00 23.02 ? 1023 HOH D O     1 
HETATM 10869 O  O     . HOH JA 6 .   ? 88.559  50.354  136.244 1.00 29.46 ? 1024 HOH D O     1 
HETATM 10870 O  O     . HOH JA 6 .   ? 82.957  78.070  135.862 1.00 20.88 ? 1025 HOH D O     1 
HETATM 10871 O  O     . HOH JA 6 .   ? 80.468  54.025  136.210 1.00 24.32 ? 1026 HOH D O     1 
HETATM 10872 O  O     . HOH JA 6 .   ? 65.478  62.392  142.181 1.00 25.95 ? 1027 HOH D O     1 
HETATM 10873 O  O     . HOH JA 6 .   ? 64.325  66.421  136.206 1.00 15.75 ? 1028 HOH D O     1 
HETATM 10874 O  O     . HOH JA 6 .   ? 94.200  49.278  104.986 1.00 44.76 ? 1029 HOH D O     1 
HETATM 10875 O  O     . HOH JA 6 .   ? 85.964  39.232  103.486 1.00 26.40 ? 1030 HOH D O     1 
HETATM 10876 O  O     . HOH JA 6 .   ? 80.936  43.422  113.404 1.00 20.06 ? 1031 HOH D O     1 
HETATM 10877 O  O     . HOH JA 6 .   ? 94.023  42.269  109.395 1.00 34.04 ? 1032 HOH D O     1 
HETATM 10878 O  O     . HOH JA 6 .   ? 85.527  58.149  109.475 1.00 32.76 ? 1033 HOH D O     1 
HETATM 10879 O  O     . HOH JA 6 .   ? 96.957  48.131  107.048 1.00 53.58 ? 1034 HOH D O     1 
HETATM 10880 O  O     . HOH JA 6 .   ? 94.450  66.129  111.117 1.00 28.92 ? 1035 HOH D O     1 
HETATM 10881 O  O     . HOH JA 6 .   ? 85.815  32.233  111.396 1.00 23.35 ? 1036 HOH D O     1 
HETATM 10882 O  O     . HOH JA 6 .   ? 78.708  43.117  111.816 1.00 31.14 ? 1037 HOH D O     1 
HETATM 10883 O  O     . HOH JA 6 .   ? 94.303  61.276  112.964 1.00 31.63 ? 1038 HOH D O     1 
HETATM 10884 O  O     . HOH JA 6 .   ? 86.538  31.358  115.048 1.00 36.29 ? 1039 HOH D O     1 
HETATM 10885 O  O     . HOH JA 6 .   ? 89.585  32.175  113.539 1.00 27.31 ? 1040 HOH D O     1 
HETATM 10886 O  O     . HOH JA 6 .   ? 99.783  42.966  115.418 1.00 34.60 ? 1041 HOH D O     1 
HETATM 10887 O  O     . HOH JA 6 .   ? 97.694  56.923  115.748 1.00 20.66 ? 1042 HOH D O     1 
HETATM 10888 O  O     . HOH JA 6 .   ? 93.233  47.314  117.728 1.00 16.06 ? 1043 HOH D O     1 
HETATM 10889 O  O     . HOH JA 6 .   ? 95.654  44.618  127.543 1.00 28.78 ? 1044 HOH D O     1 
HETATM 10890 O  O     . HOH JA 6 .   ? 98.412  38.725  113.798 1.00 34.34 ? 1045 HOH D O     1 
HETATM 10891 O  O     . HOH JA 6 .   ? 82.476  39.198  114.791 1.00 40.99 ? 1046 HOH D O     1 
HETATM 10892 O  O     . HOH JA 6 .   ? 95.103  32.543  119.553 1.00 51.04 ? 1047 HOH D O     1 
HETATM 10893 O  O     . HOH JA 6 .   ? 98.701  54.878  109.676 1.00 41.12 ? 1048 HOH D O     1 
HETATM 10894 O  O     . HOH JA 6 .   ? 95.938  61.410  115.166 1.00 33.93 ? 1049 HOH D O     1 
HETATM 10895 O  O     . HOH JA 6 .   ? 97.606  59.546  114.363 1.00 39.87 ? 1050 HOH D O     1 
HETATM 10896 O  O     . HOH JA 6 .   ? 103.958 53.447  117.039 1.00 32.54 ? 1051 HOH D O     1 
HETATM 10897 O  O     . HOH JA 6 .   ? 96.831  58.886  111.688 1.00 45.37 ? 1052 HOH D O     1 
HETATM 10898 O  O     . HOH JA 6 .   ? 80.907  69.766  118.837 1.00 15.50 ? 1053 HOH D O     1 
HETATM 10899 O  O     . HOH JA 6 .   ? 101.511 63.460  119.065 1.00 22.92 ? 1054 HOH D O     1 
HETATM 10900 O  O     . HOH JA 6 .   ? 76.393  42.772  120.043 1.00 31.96 ? 1055 HOH D O     1 
HETATM 10901 O  O     . HOH JA 6 .   ? 99.373  43.513  126.175 1.00 33.60 ? 1056 HOH D O     1 
HETATM 10902 O  O     . HOH JA 6 .   ? 76.476  64.094  119.531 1.00 20.40 ? 1057 HOH D O     1 
HETATM 10903 O  O     . HOH JA 6 .   ? 103.061 38.520  117.629 1.00 34.60 ? 1058 HOH D O     1 
HETATM 10904 O  O     . HOH JA 6 .   ? 70.488  59.718  110.311 1.00 48.19 ? 1059 HOH D O     1 
HETATM 10905 O  O     . HOH JA 6 .   ? 101.897 59.510  124.620 1.00 22.20 ? 1060 HOH D O     1 
HETATM 10906 O  O     . HOH JA 6 .   ? 91.215  79.185  123.985 1.00 28.88 ? 1061 HOH D O     1 
HETATM 10907 O  O     . HOH JA 6 .   ? 100.381 45.774  114.633 1.00 29.45 ? 1062 HOH D O     1 
HETATM 10908 O  O     . HOH JA 6 .   ? 86.924  42.625  122.192 1.00 17.60 ? 1063 HOH D O     1 
HETATM 10909 O  O     . HOH JA 6 .   ? 102.269 48.173  122.531 1.00 23.74 ? 1064 HOH D O     1 
HETATM 10910 O  O     . HOH JA 6 .   ? 94.368  55.397  137.458 1.00 28.58 ? 1065 HOH D O     1 
HETATM 10911 O  O     . HOH JA 6 .   ? 72.461  64.662  127.766 1.00 15.16 ? 1066 HOH D O     1 
HETATM 10912 O  O     . HOH JA 6 .   ? 104.642 51.028  119.737 1.00 45.82 ? 1067 HOH D O     1 
HETATM 10913 O  O     . HOH JA 6 .   ? 72.433  54.204  122.656 1.00 19.18 ? 1068 HOH D O     1 
HETATM 10914 O  O     . HOH JA 6 .   ? 103.192 48.634  120.155 1.00 30.44 ? 1069 HOH D O     1 
HETATM 10915 O  O     . HOH JA 6 .   ? 88.635  30.831  123.358 1.00 30.78 ? 1070 HOH D O     1 
HETATM 10916 O  O     . HOH JA 6 .   ? 88.617  35.371  123.930 1.00 23.12 ? 1071 HOH D O     1 
HETATM 10917 O  O     . HOH JA 6 .   ? 95.215  38.107  123.862 1.00 26.02 ? 1072 HOH D O     1 
HETATM 10918 O  O     . HOH JA 6 .   ? 72.855  40.362  124.215 1.00 36.76 ? 1073 HOH D O     1 
HETATM 10919 O  O     . HOH JA 6 .   ? 99.050  41.880  124.144 1.00 20.07 ? 1074 HOH D O     1 
HETATM 10920 O  O     . HOH JA 6 .   ? 75.612  50.001  136.701 1.00 23.44 ? 1075 HOH D O     1 
HETATM 10921 O  O     . HOH JA 6 .   ? 76.879  64.578  124.824 1.00 16.76 ? 1076 HOH D O     1 
HETATM 10922 O  O     . HOH JA 6 .   ? 77.364  63.972  122.160 1.00 19.16 ? 1077 HOH D O     1 
HETATM 10923 O  O     . HOH JA 6 .   ? 96.310  74.533  126.895 1.00 47.85 ? 1078 HOH D O     1 
HETATM 10924 O  O     . HOH JA 6 .   ? 105.377 37.431  124.837 1.00 48.65 ? 1079 HOH D O     1 
HETATM 10925 O  O     . HOH JA 6 .   ? 98.135  37.042  125.945 1.00 22.73 ? 1080 HOH D O     1 
HETATM 10926 O  O     . HOH JA 6 .   ? 72.388  42.755  124.833 1.00 31.71 ? 1081 HOH D O     1 
HETATM 10927 O  O     . HOH JA 6 .   ? 92.314  64.199  133.827 1.00 45.27 ? 1082 HOH D O     1 
HETATM 10928 O  O     . HOH JA 6 .   ? 67.601  51.080  140.803 1.00 34.97 ? 1083 HOH D O     1 
HETATM 10929 O  O     . HOH JA 6 .   ? 93.515  39.383  130.238 1.00 22.44 ? 1084 HOH D O     1 
HETATM 10930 O  O     . HOH JA 6 .   ? 96.013  63.044  124.732 1.00 27.16 ? 1085 HOH D O     1 
HETATM 10931 O  O     . HOH JA 6 .   ? 91.713  61.703  137.023 1.00 35.43 ? 1086 HOH D O     1 
HETATM 10932 O  O     . HOH JA 6 .   ? 77.591  71.525  126.961 1.00 19.95 ? 1087 HOH D O     1 
HETATM 10933 O  O     . HOH JA 6 .   ? 72.589  43.923  122.546 1.00 35.58 ? 1088 HOH D O     1 
HETATM 10934 O  O     . HOH JA 6 .   ? 77.380  67.053  122.555 1.00 29.76 ? 1089 HOH D O     1 
HETATM 10935 O  O     . HOH JA 6 .   ? 71.572  72.871  135.491 1.00 23.97 ? 1090 HOH D O     1 
HETATM 10936 O  O     . HOH JA 6 .   ? 101.239 54.766  129.065 1.00 27.67 ? 1091 HOH D O     1 
HETATM 10937 O  O     . HOH JA 6 .   ? 102.817 56.872  128.758 1.00 35.06 ? 1092 HOH D O     1 
HETATM 10938 O  O     . HOH JA 6 .   ? 65.995  57.832  129.684 1.00 40.08 ? 1093 HOH D O     1 
HETATM 10939 O  O     . HOH JA 6 .   ? 77.362  91.500  130.171 1.00 27.30 ? 1094 HOH D O     1 
HETATM 10940 O  O     . HOH JA 6 .   ? 95.791  65.911  130.569 1.00 33.42 ? 1095 HOH D O     1 
HETATM 10941 O  O     . HOH JA 6 .   ? 74.280  56.452  137.302 1.00 28.31 ? 1096 HOH D O     1 
HETATM 10942 O  O     . HOH JA 6 .   ? 76.178  56.036  131.372 1.00 33.20 ? 1097 HOH D O     1 
HETATM 10943 O  O     . HOH JA 6 .   ? 73.232  51.250  137.009 1.00 22.89 ? 1098 HOH D O     1 
HETATM 10944 O  O     . HOH JA 6 .   ? 92.375  77.591  126.142 1.00 30.71 ? 1099 HOH D O     1 
HETATM 10945 O  O     . HOH JA 6 .   ? 91.846  39.262  132.645 1.00 16.65 ? 1100 HOH D O     1 
HETATM 10946 O  O     . HOH JA 6 .   ? 90.911  68.858  135.293 1.00 26.21 ? 1101 HOH D O     1 
HETATM 10947 O  O     . HOH JA 6 .   ? 92.961  66.870  134.809 1.00 40.58 ? 1102 HOH D O     1 
HETATM 10948 O  O     . HOH JA 6 .   ? 95.852  50.288  135.167 1.00 21.53 ? 1103 HOH D O     1 
HETATM 10949 O  O     . HOH JA 6 .   ? 88.987  55.247  139.475 1.00 56.94 ? 1104 HOH D O     1 
HETATM 10950 O  O     . HOH JA 6 .   ? 67.812  50.812  128.760 1.00 24.62 ? 1105 HOH D O     1 
HETATM 10951 O  O     . HOH JA 6 .   ? 93.467  59.176  136.403 1.00 37.40 ? 1106 HOH D O     1 
HETATM 10952 O  O     . HOH JA 6 .   ? 91.114  66.688  138.674 1.00 51.84 ? 1107 HOH D O     1 
HETATM 10953 O  O     . HOH JA 6 .   ? 95.228  60.321  134.874 1.00 48.13 ? 1108 HOH D O     1 
HETATM 10954 O  O     . HOH JA 6 .   ? 79.998  51.075  135.994 1.00 23.91 ? 1109 HOH D O     1 
HETATM 10955 O  O     . HOH JA 6 .   ? 77.828  56.208  134.129 1.00 50.04 ? 1110 HOH D O     1 
HETATM 10956 O  O     . HOH JA 6 .   ? 68.630  52.481  135.861 1.00 29.82 ? 1111 HOH D O     1 
HETATM 10957 O  O     . HOH JA 6 .   ? 86.730  55.418  137.327 1.00 42.76 ? 1112 HOH D O     1 
HETATM 10958 O  O     . HOH JA 6 .   ? 84.310  80.475  135.990 1.00 29.21 ? 1113 HOH D O     1 
HETATM 10959 O  O     . HOH JA 6 .   ? 83.487  83.062  132.033 1.00 34.47 ? 1114 HOH D O     1 
HETATM 10960 O  O     . HOH JA 6 .   ? 89.474  47.768  136.368 1.00 23.83 ? 1115 HOH D O     1 
HETATM 10961 O  O     . HOH JA 6 .   ? 69.038  51.213  138.245 1.00 30.58 ? 1116 HOH D O     1 
HETATM 10962 O  O     . HOH JA 6 .   ? 92.411  39.053  135.415 1.00 17.19 ? 1117 HOH D O     1 
HETATM 10963 O  O     . HOH JA 6 .   ? 82.630  52.117  137.450 1.00 20.88 ? 1118 HOH D O     1 
HETATM 10964 O  O     . HOH JA 6 .   ? 85.234  52.050  136.925 1.00 22.65 ? 1119 HOH D O     1 
HETATM 10965 O  O     . HOH JA 6 .   ? 73.421  53.883  138.142 1.00 24.50 ? 1120 HOH D O     1 
HETATM 10966 O  O     . HOH JA 6 .   ? 97.157  37.274  129.472 1.00 34.63 ? 1121 HOH D O     1 
HETATM 10967 O  O     . HOH JA 6 .   ? 73.280  70.964  134.498 1.00 25.84 ? 1122 HOH D O     1 
HETATM 10968 O  O     . HOH JA 6 .   ? 71.024  71.978  139.302 1.00 33.76 ? 1123 HOH D O     1 
HETATM 10969 O  O     . HOH JA 6 .   ? 97.673  54.978  132.925 1.00 51.27 ? 1124 HOH D O     1 
HETATM 10970 O  O     . HOH JA 6 .   ? 106.016 59.784  122.972 1.00 40.49 ? 1125 HOH D O     1 
HETATM 10971 O  O     . HOH JA 6 .   ? 89.840  70.537  130.865 1.00 24.37 ? 1126 HOH D O     1 
HETATM 10972 O  O     . HOH JA 6 .   ? 90.701  70.808  133.451 1.00 39.00 ? 1127 HOH D O     1 
HETATM 10973 O  O     . HOH JA 6 .   ? 82.721  80.815  133.521 1.00 30.10 ? 1128 HOH D O     1 
HETATM 10974 O  O     . HOH JA 6 .   ? 86.998  79.505  139.645 1.00 41.73 ? 1129 HOH D O     1 
HETATM 10975 O  O     . HOH JA 6 .   ? 84.378  83.285  139.392 1.00 33.84 ? 1130 HOH D O     1 
HETATM 10976 O  O     . HOH JA 6 .   ? 84.855  82.061  142.697 1.00 52.71 ? 1131 HOH D O     1 
HETATM 10977 O  O     . HOH JA 6 .   ? 84.797  80.424  138.683 1.00 38.85 ? 1132 HOH D O     1 
HETATM 10978 O  O     . HOH JA 6 .   ? 89.353  73.881  139.322 1.00 51.85 ? 1133 HOH D O     1 
HETATM 10979 O  O     . HOH JA 6 .   ? 86.847  80.469  134.342 1.00 44.47 ? 1134 HOH D O     1 
HETATM 10980 O  O     . HOH JA 6 .   ? 75.810  92.859  126.636 1.00 40.43 ? 1135 HOH D O     1 
HETATM 10981 O  O     . HOH JA 6 .   ? 75.934  95.838  124.684 1.00 54.64 ? 1136 HOH D O     1 
HETATM 10982 O  O     . HOH JA 6 .   ? 84.202  89.335  127.625 1.00 42.21 ? 1137 HOH D O     1 
HETATM 10983 O  O     . HOH JA 6 .   ? 92.987  59.436  109.226 1.00 47.79 ? 1138 HOH D O     1 
HETATM 10984 O  O     . HOH JA 6 .   ? 87.234  67.898  119.439 1.00 25.61 ? 1139 HOH D O     1 
HETATM 10985 O  O     . HOH JA 6 .   ? 64.954  57.442  127.663 1.00 42.14 ? 1140 HOH D O     1 
HETATM 10986 O  O     . HOH JA 6 .   ? 62.347  60.321  138.804 1.00 36.93 ? 1141 HOH D O     1 
HETATM 10987 O  O     . HOH JA 6 .   ? 62.729  84.147  147.023 1.00 36.39 ? 1142 HOH D O     1 
HETATM 10988 O  O     . HOH JA 6 .   ? 64.824  88.435  146.210 1.00 41.47 ? 1143 HOH D O     1 
HETATM 10989 O  O     . HOH JA 6 .   ? 65.431  85.174  146.885 1.00 40.78 ? 1144 HOH D O     1 
HETATM 10990 O  O     . HOH JA 6 .   ? 70.136  77.049  143.428 1.00 37.28 ? 1145 HOH D O     1 
HETATM 10991 O  O     . HOH JA 6 .   ? 69.753  68.336  144.000 1.00 26.98 ? 1146 HOH D O     1 
HETATM 10992 O  O     . HOH JA 6 .   ? 71.017  73.586  137.834 1.00 29.89 ? 1147 HOH D O     1 
HETATM 10993 O  O     . HOH JA 6 .   ? 71.650  47.905  120.537 1.00 31.68 ? 1148 HOH D O     1 
HETATM 10994 O  O     . HOH JA 6 .   ? 73.337  44.770  115.923 1.00 42.13 ? 1149 HOH D O     1 
HETATM 10995 O  O     . HOH JA 6 .   ? 71.446  49.614  138.158 1.00 25.89 ? 1150 HOH D O     1 
HETATM 10996 O  O     . HOH JA 6 .   ? 74.616  47.487  140.779 1.00 28.70 ? 1151 HOH D O     1 
HETATM 10997 O  O     . HOH JA 6 .   ? 76.223  47.078  143.130 1.00 36.92 ? 1152 HOH D O     1 
HETATM 10998 O  O     . HOH JA 6 .   ? 77.474  46.577  146.349 1.00 60.04 ? 1153 HOH D O     1 
HETATM 10999 O  O     . HOH JA 6 .   ? 69.064  50.010  142.628 1.00 32.62 ? 1154 HOH D O     1 
HETATM 11000 O  O     . HOH JA 6 .   ? 68.334  53.757  149.070 1.00 38.24 ? 1155 HOH D O     1 
HETATM 11001 O  O     . HOH JA 6 .   ? 70.164  52.971  150.677 1.00 46.20 ? 1156 HOH D O     1 
HETATM 11002 O  O     . HOH JA 6 .   ? 101.830 63.601  116.344 1.00 31.84 ? 1157 HOH D O     1 
HETATM 11003 O  O     . HOH JA 6 .   ? 98.428  65.959  126.475 1.00 44.07 ? 1158 HOH D O     1 
HETATM 11004 O  O     . HOH JA 6 .   ? 96.048  59.317  116.070 1.00 29.93 ? 1159 HOH D O     1 
HETATM 11005 O  O     . HOH JA 6 .   ? 99.027  64.006  128.656 1.00 45.97 ? 1160 HOH D O     1 
HETATM 11006 O  O     . HOH JA 6 .   ? 101.585 64.020  127.105 1.00 50.17 ? 1161 HOH D O     1 
HETATM 11007 O  O     . HOH JA 6 .   ? 105.604 37.121  117.984 1.00 44.59 ? 1162 HOH D O     1 
HETATM 11008 O  O     . HOH JA 6 .   ? 92.874  33.139  122.058 1.00 55.25 ? 1163 HOH D O     1 
HETATM 11009 O  O     . HOH JA 6 .   ? 96.934  45.699  108.424 1.00 44.74 ? 1164 HOH D O     1 
HETATM 11010 O  O     . HOH JA 6 .   ? 103.378 48.358  112.465 1.00 50.03 ? 1165 HOH D O     1 
HETATM 11011 O  O     . HOH JA 6 .   ? 100.810 43.074  111.821 1.00 53.50 ? 1166 HOH D O     1 
HETATM 11012 O  O     . HOH JA 6 .   ? 106.691 51.360  123.436 1.00 56.12 ? 1167 HOH D O     1 
HETATM 11013 O  O     . HOH JA 6 .   ? 107.299 42.787  126.034 1.00 50.53 ? 1168 HOH D O     1 
HETATM 11014 O  O     . HOH JA 6 .   ? 108.219 43.617  121.624 1.00 36.40 ? 1169 HOH D O     1 
HETATM 11015 O  O     . HOH JA 6 .   ? 100.070 40.152  131.449 1.00 41.18 ? 1170 HOH D O     1 
HETATM 11016 O  O     . HOH JA 6 .   ? 89.414  52.348  137.647 1.00 40.99 ? 1171 HOH D O     1 
HETATM 11017 O  O     . HOH JA 6 .   ? 92.315  58.659  141.963 1.00 51.82 ? 1172 HOH D O     1 
HETATM 11018 O  O     . HOH JA 6 .   ? 97.461  43.778  126.891 1.00 52.76 ? 1173 HOH D O     1 
HETATM 11019 O  O     . HOH JA 6 .   ? 95.628  71.516  127.204 1.00 33.22 ? 1174 HOH D O     1 
HETATM 11020 O  O     . HOH JA 6 .   ? 89.290  73.518  130.814 1.00 38.35 ? 1175 HOH D O     1 
HETATM 11021 O  O     . HOH JA 6 .   ? 89.104  75.324  133.365 1.00 33.62 ? 1176 HOH D O     1 
HETATM 11022 O  O     . HOH JA 6 .   ? 90.238  74.172  136.404 1.00 44.83 ? 1177 HOH D O     1 
HETATM 11023 O  O     . HOH JA 6 .   ? 74.777  65.804  148.689 1.00 27.83 ? 1178 HOH D O     1 
HETATM 11024 O  O     . HOH JA 6 .   ? 70.818  66.057  150.311 1.00 31.58 ? 1179 HOH D O     1 
HETATM 11025 O  O     . HOH JA 6 .   ? 68.140  69.372  145.721 1.00 39.89 ? 1180 HOH D O     1 
HETATM 11026 O  O     . HOH JA 6 .   ? 66.870  62.836  154.502 1.00 39.21 ? 1181 HOH D O     1 
HETATM 11027 O  O     . HOH JA 6 .   ? 72.713  57.894  139.179 1.00 39.69 ? 1182 HOH D O     1 
HETATM 11028 O  O     . HOH JA 6 .   ? 82.526  75.366  143.034 1.00 36.67 ? 1183 HOH D O     1 
HETATM 11029 O  O     . HOH JA 6 .   ? 77.788  84.798  141.848 1.00 35.33 ? 1184 HOH D O     1 
HETATM 11030 O  O     . HOH JA 6 .   ? 82.742  88.705  143.145 1.00 36.48 ? 1185 HOH D O     1 
HETATM 11031 O  O     . HOH JA 6 .   ? 86.115  89.901  135.947 1.00 52.30 ? 1186 HOH D O     1 
HETATM 11032 O  O     . HOH JA 6 .   ? 79.961  92.780  141.166 1.00 37.69 ? 1187 HOH D O     1 
HETATM 11033 O  O     . HOH JA 6 .   ? 80.533  86.407  144.563 1.00 35.57 ? 1188 HOH D O     1 
HETATM 11034 O  O     . HOH JA 6 .   ? 75.513  98.184  130.214 1.00 42.03 ? 1189 HOH D O     1 
HETATM 11035 O  O     . HOH JA 6 .   ? 73.877  84.318  146.179 1.00 56.91 ? 1190 HOH D O     1 
HETATM 11036 O  O     . HOH JA 6 .   ? 82.672  42.025  112.547 1.00 39.89 ? 1191 HOH D O     1 
HETATM 11037 O  O     . HOH JA 6 .   ? 89.078  55.986  107.373 1.00 32.73 ? 1192 HOH D O     1 
HETATM 11038 O  O     . HOH JA 6 .   ? 93.489  55.593  108.746 1.00 56.46 ? 1193 HOH D O     1 
HETATM 11039 O  O     . HOH JA 6 .   ? 95.696  56.255  109.419 1.00 52.72 ? 1194 HOH D O     1 
HETATM 11040 O  O     . HOH JA 6 .   ? 81.343  40.330  103.557 1.00 43.64 ? 1195 HOH D O     1 
HETATM 11041 O  O     . HOH JA 6 .   ? 80.204  40.544  105.828 1.00 43.82 ? 1196 HOH D O     1 
HETATM 11042 O  O     . HOH JA 6 .   ? 81.062  41.651  107.904 1.00 35.86 ? 1197 HOH D O     1 
HETATM 11043 O  O     . HOH JA 6 .   ? 78.598  50.453  103.573 1.00 47.30 ? 1198 HOH D O     1 
HETATM 11044 O  O     . HOH JA 6 .   ? 75.185  44.575  108.926 1.00 35.15 ? 1199 HOH D O     1 
HETATM 11045 O  O     . HOH JA 6 .   ? 76.288  42.197  112.390 1.00 58.44 ? 1200 HOH D O     1 
HETATM 11046 O  O     . HOH JA 6 .   ? 87.798  51.869  145.890 1.00 37.80 ? 1201 HOH D O     1 
HETATM 11047 O  O     . HOH JA 6 .   ? 84.747  33.931  114.795 1.00 30.17 ? 1202 HOH D O     1 
HETATM 11048 O  O     . HOH JA 6 .   ? 86.378  30.553  117.692 1.00 44.06 ? 1203 HOH D O     1 
HETATM 11049 O  O     . HOH JA 6 .   ? 79.527  41.004  110.075 1.00 50.52 ? 1204 HOH D O     1 
HETATM 11050 O  O     . HOH JA 6 .   ? 85.163  83.747  123.452 1.00 34.93 ? 1205 HOH D O     1 
HETATM 11051 O  O     . HOH JA 6 .   ? 83.784  58.198  105.521 1.00 37.17 ? 1206 HOH D O     1 
HETATM 11052 O  O     . HOH JA 6 .   ? 65.175  81.190  149.759 1.00 52.87 ? 1207 HOH D O     1 
HETATM 11053 O  O     . HOH JA 6 .   ? 67.827  81.303  150.217 1.00 57.68 ? 1208 HOH D O     1 
HETATM 11054 O  O     . HOH JA 6 .   ? 66.957  84.139  148.949 1.00 52.74 ? 1209 HOH D O     1 
HETATM 11055 O  O     . HOH JA 6 .   ? 70.490  47.808  142.499 1.00 43.29 ? 1210 HOH D O     1 
HETATM 11056 O  O     . HOH JA 6 .   ? 70.125  50.736  152.320 1.00 52.61 ? 1211 HOH D O     1 
HETATM 11057 O  O     . HOH JA 6 .   ? 102.739 67.979  123.233 1.00 45.63 ? 1212 HOH D O     1 
HETATM 11058 O  O     . HOH JA 6 .   ? 101.153 57.509  113.064 1.00 49.23 ? 1213 HOH D O     1 
HETATM 11059 O  O     . HOH JA 6 .   ? 101.232 49.758  131.786 1.00 40.43 ? 1214 HOH D O     1 
HETATM 11060 O  O     . HOH JA 6 .   ? 99.367  50.401  133.373 1.00 53.78 ? 1215 HOH D O     1 
HETATM 11061 O  O     . HOH JA 6 .   ? 99.007  53.437  131.499 1.00 49.92 ? 1216 HOH D O     1 
HETATM 11062 O  O     . HOH JA 6 .   ? 105.371 42.901  116.134 1.00 56.16 ? 1217 HOH D O     1 
HETATM 11063 O  O     . HOH JA 6 .   ? 65.558  57.363  143.324 1.00 55.60 ? 1218 HOH D O     1 
HETATM 11064 O  O     . HOH JA 6 .   ? 77.000  56.352  136.867 1.00 36.82 ? 1219 HOH D O     1 
HETATM 11065 O  O     . HOH JA 6 .   ? 92.047  64.692  137.468 1.00 58.22 ? 1220 HOH D O     1 
HETATM 11066 O  O     . HOH JA 6 .   ? 66.664  88.716  148.452 1.00 48.38 ? 1221 HOH D O     1 
HETATM 11067 O  O     . HOH JA 6 .   ? 73.492  96.208  144.616 1.00 48.00 ? 1222 HOH D O     1 
HETATM 11068 O  O     . HOH JA 6 .   ? 65.083  66.659  147.324 1.00 35.28 ? 1223 HOH D O     1 
HETATM 11069 O  O     . HOH JA 6 .   ? 85.500  47.373  100.764 1.00 43.29 ? 1224 HOH D O     1 
HETATM 11070 O  O     . HOH JA 6 .   ? 91.150  50.964  103.320 1.00 36.27 ? 1225 HOH D O     1 
HETATM 11071 O  O     . HOH JA 6 .   ? 84.344  49.545  100.051 1.00 60.04 ? 1226 HOH D O     1 
HETATM 11072 O  O     . HOH JA 6 .   ? 72.833  53.443  106.965 1.00 49.72 ? 1227 HOH D O     1 
HETATM 11073 O  O     . HOH JA 6 .   ? 74.824  51.328  106.014 1.00 38.43 ? 1228 HOH D O     1 
HETATM 11074 O  O     . HOH JA 6 .   ? 77.754  55.816  103.561 1.00 47.79 ? 1229 HOH D O     1 
HETATM 11075 O  O     . HOH JA 6 .   ? 76.552  46.776  101.449 1.00 51.72 ? 1230 HOH D O     1 
HETATM 11076 O  O     . HOH JA 6 .   ? 88.145  27.353  122.716 1.00 55.33 ? 1231 HOH D O     1 
HETATM 11077 O  O     . HOH JA 6 .   ? 94.585  64.956  133.393 1.00 46.40 ? 1232 HOH D O     1 
HETATM 11078 O  O     . HOH JA 6 .   ? 71.862  50.685  150.648 1.00 56.21 ? 1233 HOH D O     1 
HETATM 11079 O  O     . HOH JA 6 .   ? 76.046  46.189  148.227 1.00 59.77 ? 1234 HOH D O     1 
HETATM 11080 O  O     . HOH JA 6 .   ? 78.594  87.293  147.073 1.00 55.47 ? 1235 HOH D O     1 
HETATM 11081 O  O     . HOH JA 6 .   ? 83.729  38.505  104.514 1.00 49.50 ? 1236 HOH D O     1 
HETATM 11082 O  O     . HOH JA 6 .   ? 90.028  33.464  123.006 1.00 38.84 ? 1237 HOH D O     1 
HETATM 11083 O  O     . HOH JA 6 .   ? 78.456  60.833  107.579 1.00 47.99 ? 1238 HOH D O     1 
HETATM 11084 O  O     . HOH JA 6 .   ? 76.057  64.826  115.927 1.00 36.38 ? 1239 HOH D O     1 
HETATM 11085 O  O     . HOH JA 6 .   ? 57.430  53.955  157.264 1.00 45.07 ? 1240 HOH D O     1 
HETATM 11086 O  O     . HOH JA 6 .   ? 75.047  45.133  131.684 1.00 32.62 ? 1241 HOH D O     1 
HETATM 11087 O  O     . HOH JA 6 .   ? 71.232  45.922  122.072 1.00 40.16 ? 1242 HOH D O     1 
HETATM 11088 O  O     . HOH JA 6 .   ? 63.292  52.728  141.801 1.00 29.72 ? 1243 HOH D O     1 
HETATM 11089 O  O     . HOH JA 6 .   ? 99.729  63.857  115.162 1.00 53.90 ? 1244 HOH D O     1 
HETATM 11090 O  O     . HOH JA 6 .   ? 102.776 60.881  126.792 1.00 40.76 ? 1245 HOH D O     1 
HETATM 11091 O  O     . HOH JA 6 .   ? 105.184 49.020  129.369 1.00 44.26 ? 1246 HOH D O     1 
HETATM 11092 O  O     . HOH JA 6 .   ? 104.304 58.417  127.817 1.00 51.89 ? 1247 HOH D O     1 
HETATM 11093 O  O     . HOH JA 6 .   ? 98.822  40.739  114.880 1.00 54.19 ? 1248 HOH D O     1 
HETATM 11094 O  O     . HOH JA 6 .   ? 102.442 59.406  130.223 1.00 54.01 ? 1249 HOH D O     1 
HETATM 11095 O  O     . HOH JA 6 .   ? 104.332 39.484  128.170 1.00 35.83 ? 1250 HOH D O     1 
HETATM 11096 O  O     . HOH JA 6 .   ? 106.040 49.392  118.599 1.00 49.06 ? 1251 HOH D O     1 
HETATM 11097 O  O     . HOH JA 6 .   ? 95.133  35.258  123.523 1.00 51.15 ? 1252 HOH D O     1 
HETATM 11098 O  O     . HOH JA 6 .   ? 99.105  35.407  129.546 1.00 42.10 ? 1253 HOH D O     1 
HETATM 11099 O  O     . HOH JA 6 .   ? 107.558 32.096  124.051 1.00 51.12 ? 1254 HOH D O     1 
HETATM 11100 O  O     . HOH JA 6 .   ? 96.111  33.680  122.259 1.00 43.79 ? 1255 HOH D O     1 
HETATM 11101 O  O     . HOH JA 6 .   ? 90.977  32.945  115.868 1.00 37.01 ? 1256 HOH D O     1 
HETATM 11102 O  O     . HOH JA 6 .   ? 88.021  29.355  121.209 1.00 47.15 ? 1257 HOH D O     1 
HETATM 11103 O  O     . HOH JA 6 .   ? 102.475 47.731  108.657 1.00 58.79 ? 1258 HOH D O     1 
HETATM 11104 O  O     . HOH JA 6 .   ? 106.202 41.840  128.002 1.00 54.24 ? 1259 HOH D O     1 
HETATM 11105 O  O     . HOH JA 6 .   ? 99.238  42.218  140.303 1.00 41.98 ? 1260 HOH D O     1 
HETATM 11106 O  O     . HOH JA 6 .   ? 99.247  58.163  131.424 1.00 51.69 ? 1261 HOH D O     1 
HETATM 11107 O  O     . HOH JA 6 .   ? 91.403  69.839  137.564 1.00 60.03 ? 1262 HOH D O     1 
HETATM 11108 O  O     . HOH JA 6 .   ? 87.056  53.806  140.904 1.00 60.01 ? 1263 HOH D O     1 
HETATM 11109 O  O     . HOH JA 6 .   ? 92.107  64.685  139.916 1.00 60.04 ? 1264 HOH D O     1 
HETATM 11110 O  O     . HOH JA 6 .   ? 83.112  52.162  145.587 1.00 53.77 ? 1265 HOH D O     1 
HETATM 11111 O  O     . HOH JA 6 .   ? 83.579  68.930  144.723 1.00 53.44 ? 1266 HOH D O     1 
HETATM 11112 O  O     . HOH JA 6 .   ? 81.656  52.780  139.411 1.00 35.53 ? 1267 HOH D O     1 
HETATM 11113 O  O     . HOH JA 6 .   ? 80.498  69.301  146.427 1.00 39.52 ? 1268 HOH D O     1 
HETATM 11114 O  O     . HOH JA 6 .   ? 68.878  82.637  147.968 1.00 57.22 ? 1269 HOH D O     1 
HETATM 11115 O  O     . HOH JA 6 .   ? 81.391  51.767  142.073 1.00 48.45 ? 1270 HOH D O     1 
HETATM 11116 O  O     . HOH JA 6 .   ? 87.913  72.382  142.193 1.00 44.62 ? 1271 HOH D O     1 
HETATM 11117 O  O     . HOH JA 6 .   ? 85.338  87.941  143.478 1.00 43.53 ? 1272 HOH D O     1 
HETATM 11118 O  O     . HOH JA 6 .   ? 76.393  85.994  146.453 1.00 51.91 ? 1273 HOH D O     1 
HETATM 11119 O  O     . HOH JA 6 .   ? 86.621  87.630  137.083 1.00 48.51 ? 1274 HOH D O     1 
HETATM 11120 O  O     . HOH JA 6 .   ? 81.282  91.516  142.987 1.00 47.60 ? 1275 HOH D O     1 
HETATM 11121 O  O     . HOH JA 6 .   ? 80.307  96.078  136.154 1.00 55.67 ? 1276 HOH D O     1 
HETATM 11122 O  O     . HOH JA 6 .   ? 69.198  95.381  145.446 1.00 45.46 ? 1277 HOH D O     1 
HETATM 11123 O  O     . HOH JA 6 .   ? 68.831  92.379  150.617 1.00 60.04 ? 1278 HOH D O     1 
HETATM 11124 O  O     . HOH JA 6 .   ? 81.263  41.181  114.280 1.00 43.05 ? 1279 HOH D O     1 
HETATM 11125 O  O     . HOH JA 6 .   ? 99.477  61.768  113.953 1.00 36.54 ? 1280 HOH D O     1 
HETATM 11126 O  O     . HOH JA 6 .   ? 105.240 49.220  124.089 1.00 39.95 ? 1281 HOH D O     1 
HETATM 11127 O  O     . HOH JA 6 .   ? 102.960 43.490  116.238 1.00 46.10 ? 1282 HOH D O     1 
HETATM 11128 O  O     . HOH JA 6 .   ? 102.224 49.592  110.350 1.00 54.33 ? 1283 HOH D O     1 
HETATM 11129 O  O     . HOH JA 6 .   ? 96.697  38.106  131.661 1.00 53.25 ? 1284 HOH D O     1 
HETATM 11130 O  O     . HOH JA 6 .   ? 103.670 44.025  129.338 1.00 37.01 ? 1285 HOH D O     1 
HETATM 11131 O  O     . HOH JA 6 .   ? 93.178  62.227  134.668 1.00 51.80 ? 1286 HOH D O     1 
HETATM 11132 O  O     . HOH JA 6 .   ? 89.017  75.242  129.049 1.00 34.38 ? 1287 HOH D O     1 
HETATM 11133 O  O     . HOH JA 6 .   ? 73.448  60.107  152.818 1.00 44.48 ? 1288 HOH D O     1 
HETATM 11134 O  O     . HOH JA 6 .   ? 73.426  47.305  144.862 1.00 43.85 ? 1289 HOH D O     1 
HETATM 11135 O  O     . HOH JA 6 .   ? 102.820 67.525  114.652 1.00 47.15 ? 1290 HOH D O     1 
HETATM 11136 O  O     . HOH JA 6 .   ? 97.042  63.027  126.959 1.00 42.93 ? 1291 HOH D O     1 
HETATM 11137 O  O     . HOH JA 6 .   ? 94.368  58.673  111.824 1.00 46.80 ? 1292 HOH D O     1 
HETATM 11138 O  O     . HOH JA 6 .   ? 98.792  41.390  137.813 1.00 42.77 ? 1293 HOH D O     1 
HETATM 11139 O  O     . HOH JA 6 .   ? 98.692  44.038  136.020 1.00 37.50 ? 1294 HOH D O     1 
HETATM 11140 O  O     . HOH JA 6 .   ? 100.209 44.140  134.410 1.00 45.94 ? 1295 HOH D O     1 
HETATM 11141 O  O     . HOH JA 6 .   ? 97.871  70.505  126.255 1.00 47.24 ? 1296 HOH D O     1 
HETATM 11142 O  O     . HOH JA 6 .   ? 87.654  53.496  138.265 1.00 49.40 ? 1297 HOH D O     1 
HETATM 11143 O  O     . HOH JA 6 .   ? 77.768  58.897  142.381 1.00 41.86 ? 1298 HOH D O     1 
HETATM 11144 O  O     . HOH JA 6 .   ? 80.389  46.801  129.974 1.00 45.81 ? 1299 HOH D O     1 
HETATM 11145 O  O     . HOH JA 6 .   ? 76.122  57.556  133.460 1.00 41.48 ? 1300 HOH D O     1 
HETATM 11146 O  O     . HOH JA 6 .   ? 82.276  39.944  107.058 1.00 55.19 ? 1301 HOH D O     1 
HETATM 11147 O  O     . HOH JA 6 .   ? 79.121  57.693  104.341 1.00 49.22 ? 1302 HOH D O     1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   DT  1   1   1   DT  T   E . n 
A 1 2   DG  2   2   2   DG  G   E . n 
A 1 3   DC  3   3   3   DC  C   E . n 
A 1 4   DG  4   4   4   DG  G   E . n 
B 2 1   DC  1   5   5   DC  C   I . n 
B 2 2   DC  2   6   6   DC  C   I . n 
B 2 3   DG  3   7   7   DG  G   I . n 
B 2 4   DG  4   8   8   DG  G   I . n 
B 2 5   DC  5   9   9   DC  C   I . n 
B 2 6   DG  6   10  10  DG  G   I . n 
B 2 7   DC  7   11  11  DC  C   I . n 
C 1 1   DT  1   1   1   DT  T   F . n 
C 1 2   DG  2   2   2   DG  G   F . n 
C 1 3   DC  3   3   3   DC  C   F . n 
C 1 4   DG  4   4   4   DG  G   F . n 
D 2 1   DC  1   5   5   DC  C   J . n 
D 2 2   DC  2   6   6   DC  C   J . n 
D 2 3   DG  3   7   7   DG  G   J . n 
D 2 4   DG  4   8   8   DG  G   J . n 
D 2 5   DC  5   9   9   DC  C   J . n 
D 2 6   DG  6   10  10  DG  G   J . n 
D 2 7   DC  7   11  11  DC  C   J . n 
E 1 1   DT  1   1   1   DT  T   G . n 
E 1 2   DG  2   2   2   DG  G   G . n 
E 1 3   DC  3   3   3   DC  C   G . n 
E 1 4   DG  4   4   4   DG  G   G . n 
F 2 1   DC  1   5   5   DC  C   K . n 
F 2 2   DC  2   6   6   DC  C   K . n 
F 2 3   DG  3   7   7   DG  G   K . n 
F 2 4   DG  4   8   8   DG  G   K . n 
F 2 5   DC  5   9   9   DC  C   K . n 
F 2 6   DG  6   10  10  DG  G   K . n 
F 2 7   DC  7   11  11  DC  C   K . n 
G 1 1   DT  1   1   1   DT  T   H . n 
G 1 2   DG  2   2   2   DG  G   H . n 
G 1 3   DC  3   3   3   DC  C   H . n 
G 1 4   DG  4   4   4   DG  G   H . n 
H 2 1   DC  1   5   5   DC  C   L . n 
H 2 2   DC  2   6   6   DC  C   L . n 
H 2 3   DG  3   7   7   DG  G   L . n 
H 2 4   DG  4   8   8   DG  G   L . n 
H 2 5   DC  5   9   9   DC  C   L . n 
H 2 6   DG  6   10  10  DG  G   L . n 
H 2 7   DC  7   11  11  DC  C   L . n 
I 3 1   MET 1   1   1   MET MET A . n 
I 3 2   GLN 2   2   2   GLN GLN A . n 
I 3 3   PRO 3   3   3   PRO PRO A . n 
I 3 4   LEU 4   4   4   LEU LEU A . n 
I 3 5   PHE 5   5   5   PHE PHE A . n 
I 3 6   THR 6   6   6   THR THR A . n 
I 3 7   GLN 7   7   7   GLN GLN A . n 
I 3 8   GLU 8   8   8   GLU GLU A . n 
I 3 9   ARG 9   9   9   ARG ARG A . n 
I 3 10  ARG 10  10  10  ARG ARG A . n 
I 3 11  ILE 11  11  11  ILE ILE A . n 
I 3 12  PHE 12  12  12  PHE PHE A . n 
I 3 13  HIS 13  13  13  HIS HIS A . n 
I 3 14  LYS 14  14  14  LYS LYS A . n 
I 3 15  LYS 15  15  15  LYS LYS A . n 
I 3 16  LEU 16  16  16  LEU LEU A . n 
I 3 17  LEU 17  17  17  LEU LEU A . n 
I 3 18  ASP 18  18  18  ASP ASP A . n 
I 3 19  GLY 19  19  19  GLY GLY A . n 
I 3 20  ASN 20  20  20  ASN ASN A . n 
I 3 21  ILE 21  21  21  ILE ILE A . n 
I 3 22  LEU 22  22  22  LEU LEU A . n 
I 3 23  ALA 23  23  23  ALA ALA A . n 
I 3 24  THR 24  24  24  THR THR A . n 
I 3 25  ASN 25  25  25  ASN ASN A . n 
I 3 26  ASN 26  26  26  ASN ASN A . n 
I 3 27  ARG 27  27  27  ARG ARG A . n 
I 3 28  GLY 28  28  28  GLY GLY A . n 
I 3 29  VAL 29  29  29  VAL VAL A . n 
I 3 30  VAL 30  30  30  VAL VAL A . n 
I 3 31  SER 31  31  31  SER SER A . n 
I 3 32  ASN 32  32  32  ASN ASN A . n 
I 3 33  ALA 33  33  33  ALA ALA A . n 
I 3 34  ASP 34  34  34  ASP ASP A . n 
I 3 35  GLY 35  35  35  GLY GLY A . n 
I 3 36  SER 36  36  36  SER SER A . n 
I 3 37  ASN 37  37  37  ASN ASN A . n 
I 3 38  THR 38  38  38  THR THR A . n 
I 3 39  ARG 39  39  39  ARG ARG A . n 
I 3 40  SER 40  40  40  SER SER A . n 
I 3 41  PHE 41  41  41  PHE PHE A . n 
I 3 42  ASN 42  42  42  ASN ASN A . n 
I 3 43  ILE 43  43  43  ILE ILE A . n 
I 3 44  ALA 44  44  44  ALA ALA A . n 
I 3 45  LYS 45  45  45  LYS LYS A . n 
I 3 46  GLY 46  46  46  GLY GLY A . n 
I 3 47  ILE 47  47  47  ILE ILE A . n 
I 3 48  ALA 48  48  48  ALA ALA A . n 
I 3 49  ASP 49  49  49  ASP ASP A . n 
I 3 50  LEU 50  50  50  LEU LEU A . n 
I 3 51  LEU 51  51  51  LEU LEU A . n 
I 3 52  HIS 52  52  52  HIS HIS A . n 
I 3 53  SER 53  53  53  SER SER A . n 
I 3 54  GLU 54  54  54  GLU GLU A . n 
I 3 55  THR 55  55  55  THR THR A . n 
I 3 56  VAL 56  56  56  VAL VAL A . n 
I 3 57  SER 57  57  57  SER SER A . n 
I 3 58  GLU 58  58  58  GLU GLU A . n 
I 3 59  ARG 59  59  59  ARG ARG A . n 
I 3 60  LEU 60  60  60  LEU LEU A . n 
I 3 61  PRO 61  61  61  PRO PRO A . n 
I 3 62  GLY 62  62  62  GLY GLY A . n 
I 3 63  GLN 63  63  63  GLN GLN A . n 
I 3 64  THR 64  64  64  THR THR A . n 
I 3 65  SER 65  65  65  SER SER A . n 
I 3 66  GLY 66  66  66  GLY GLY A . n 
I 3 67  ASN 67  67  67  ASN ASN A . n 
I 3 68  ALA 68  68  68  ALA ALA A . n 
I 3 69  PHE 69  69  69  PHE PHE A . n 
I 3 70  GLU 70  70  70  GLU GLU A . n 
I 3 71  ALA 71  71  71  ALA ALA A . n 
I 3 72  ILE 72  72  72  ILE ILE A . n 
I 3 73  CYS 73  73  73  CYS CYS A . n 
I 3 74  SER 74  74  74  SER SER A . n 
I 3 75  GLU 75  75  75  GLU GLU A . n 
I 3 76  PHE 76  76  76  PHE PHE A . n 
I 3 77  VAL 77  77  77  VAL VAL A . n 
I 3 78  GLN 78  78  78  GLN GLN A . n 
I 3 79  SER 79  79  79  SER SER A . n 
I 3 80  ALA 80  80  80  ALA ALA A . n 
I 3 81  PHE 81  81  81  PHE PHE A . n 
I 3 82  GLU 82  82  82  GLU GLU A . n 
I 3 83  LYS 83  83  83  LYS LYS A . n 
I 3 84  LEU 84  84  84  LEU LEU A . n 
I 3 85  GLN 85  85  85  GLN GLN A . n 
I 3 86  HIS 86  86  86  HIS HIS A . n 
I 3 87  ILE 87  87  87  ILE ILE A . n 
I 3 88  ARG 88  88  88  ARG ARG A . n 
I 3 89  PRO 89  89  89  PRO PRO A . n 
I 3 90  GLY 90  90  90  GLY GLY A . n 
I 3 91  ASP 91  91  91  ASP ASP A . n 
I 3 92  TRP 92  92  92  TRP TRP A . n 
I 3 93  ASN 93  93  93  ASN ASN A . n 
I 3 94  VAL 94  94  94  VAL VAL A . n 
I 3 95  LYS 95  95  95  LYS LYS A . n 
I 3 96  GLN 96  96  96  GLN GLN A . n 
I 3 97  VAL 97  97  97  VAL VAL A . n 
I 3 98  GLY 98  98  98  GLY GLY A . n 
I 3 99  SER 99  99  99  SER SER A . n 
I 3 100 ARG 100 100 100 ARG ARG A . n 
I 3 101 ASN 101 101 101 ASN ASN A . n 
I 3 102 ARG 102 102 102 ARG ARG A . n 
I 3 103 LEU 103 103 103 LEU LEU A . n 
I 3 104 GLU 104 104 104 GLU GLU A . n 
I 3 105 ILE 105 105 105 ILE ILE A . n 
I 3 106 ALA 106 106 106 ALA ALA A . n 
I 3 107 ARG 107 107 107 ARG ARG A . n 
I 3 108 TYR 108 108 108 TYR TYR A . n 
I 3 109 GLN 109 109 109 GLN GLN A . n 
I 3 110 GLN 110 110 110 GLN GLN A . n 
I 3 111 TYR 111 111 111 TYR TYR A . n 
I 3 112 ALA 112 112 112 ALA ALA A . n 
I 3 113 HIS 113 113 113 HIS HIS A . n 
I 3 114 LEU 114 114 114 LEU LEU A . n 
I 3 115 THR 115 115 115 THR THR A . n 
I 3 116 ALA 116 116 116 ALA ALA A . n 
I 3 117 LEU 117 117 117 LEU LEU A . n 
I 3 118 ALA 118 118 118 ALA ALA A . n 
I 3 119 LYS 119 119 119 LYS LYS A . n 
I 3 120 ALA 120 120 120 ALA ALA A . n 
I 3 121 ALA 121 121 121 ALA ALA A . n 
I 3 122 GLU 122 122 122 GLU GLU A . n 
I 3 123 GLU 123 123 123 GLU GLU A . n 
I 3 124 ASN 124 124 124 ASN ASN A . n 
I 3 125 PRO 125 125 125 PRO PRO A . n 
I 3 126 GLU 126 126 126 GLU GLU A . n 
I 3 127 LEU 127 127 127 LEU LEU A . n 
I 3 128 ALA 128 128 128 ALA ALA A . n 
I 3 129 ALA 129 129 129 ALA ALA A . n 
I 3 130 ALA 130 130 130 ALA ALA A . n 
I 3 131 LEU 131 131 131 LEU LEU A . n 
I 3 132 GLY 132 132 132 GLY GLY A . n 
I 3 133 SER 133 133 133 SER SER A . n 
I 3 134 ASP 134 134 134 ASP ASP A . n 
I 3 135 TYR 135 135 135 TYR TYR A . n 
I 3 136 THR 136 136 136 THR THR A . n 
I 3 137 ILE 137 137 137 ILE ILE A . n 
I 3 138 THR 138 138 138 THR THR A . n 
I 3 139 PRO 139 139 139 PRO PRO A . n 
I 3 140 ASP 140 140 140 ASP ASP A . n 
I 3 141 ILE 141 141 141 ILE ILE A . n 
I 3 142 ILE 142 142 142 ILE ILE A . n 
I 3 143 VAL 143 143 143 VAL VAL A . n 
I 3 144 THR 144 144 144 THR THR A . n 
I 3 145 ARG 145 145 145 ARG ARG A . n 
I 3 146 ASN 146 146 146 ASN ASN A . n 
I 3 147 LEU 147 147 147 LEU LEU A . n 
I 3 148 ILE 148 148 148 ILE ILE A . n 
I 3 149 ALA 149 149 149 ALA ALA A . n 
I 3 150 ASP 150 150 150 ASP ASP A . n 
I 3 151 ALA 151 151 151 ALA ALA A . n 
I 3 152 GLU 152 152 152 GLU GLU A . n 
I 3 153 ILE 153 153 153 ILE ILE A . n 
I 3 154 ASN 154 154 154 ASN ASN A . n 
I 3 155 ARG 155 155 155 ARG ARG A . n 
I 3 156 ASN 156 156 156 ASN ASN A . n 
I 3 157 GLU 157 157 157 GLU GLU A . n 
I 3 158 PHE 158 158 158 PHE PHE A . n 
I 3 159 LEU 159 159 159 LEU LEU A . n 
I 3 160 VAL 160 160 160 VAL VAL A . n 
I 3 161 ASP 161 161 161 ASP ASP A . n 
I 3 162 GLU 162 162 162 GLU GLU A . n 
I 3 163 ASN 163 163 163 ASN ASN A . n 
I 3 164 ILE 164 164 164 ILE ILE A . n 
I 3 165 ALA 165 165 165 ALA ALA A . n 
I 3 166 THR 166 166 166 THR THR A . n 
I 3 167 TYR 167 167 167 TYR TYR A . n 
I 3 168 ALA 168 168 168 ALA ALA A . n 
I 3 169 SER 169 169 169 SER SER A . n 
I 3 170 LEU 170 170 170 LEU LEU A . n 
I 3 171 ARG 171 171 171 ARG ARG A . n 
I 3 172 ALA 172 172 172 ALA ALA A . n 
I 3 173 GLY 173 173 173 GLY GLY A . n 
I 3 174 ASN 174 174 174 ASN ASN A . n 
I 3 175 GLY 175 175 175 GLY GLY A . n 
I 3 176 ASN 176 176 176 ASN ASN A . n 
I 3 177 MET 177 177 177 MET MET A . n 
I 3 178 PRO 178 178 178 PRO PRO A . n 
I 3 179 LEU 179 179 179 LEU LEU A . n 
I 3 180 LEU 180 180 180 LEU LEU A . n 
I 3 181 HIS 181 181 181 HIS HIS A . n 
I 3 182 ALA 182 182 182 ALA ALA A . n 
I 3 183 SER 183 183 183 SER SER A . n 
I 3 184 ILE 184 184 184 ILE ILE A . n 
I 3 185 SER 185 185 185 SER SER A . n 
I 3 186 CYS 186 186 186 CYS CYS A . n 
I 3 187 LYS 187 187 187 LYS LYS A . n 
I 3 188 TRP 188 188 188 TRP TRP A . n 
I 3 189 THR 189 189 189 THR THR A . n 
I 3 190 ILE 190 190 190 ILE ILE A . n 
I 3 191 ARG 191 191 191 ARG ARG A . n 
I 3 192 SER 192 192 192 SER SER A . n 
I 3 193 ASP 193 193 193 ASP ASP A . n 
I 3 194 ARG 194 194 194 ARG ARG A . n 
I 3 195 ALA 195 195 195 ALA ALA A . n 
I 3 196 GLN 196 196 196 GLN GLN A . n 
I 3 197 ASN 197 197 197 ASN ASN A . n 
I 3 198 ALA 198 198 198 ALA ALA A . n 
I 3 199 ARG 199 199 199 ARG ARG A . n 
I 3 200 SER 200 200 200 SER SER A . n 
I 3 201 GLU 201 201 201 GLU GLU A . n 
I 3 202 GLY 202 202 202 GLY GLY A . n 
I 3 203 LEU 203 203 203 LEU LEU A . n 
I 3 204 ASN 204 204 204 ASN ASN A . n 
I 3 205 LEU 205 205 205 LEU LEU A . n 
I 3 206 VAL 206 206 206 VAL VAL A . n 
I 3 207 ARG 207 207 207 ARG ARG A . n 
I 3 208 ASN 208 208 208 ASN ASN A . n 
I 3 209 ARG 209 209 209 ARG ARG A . n 
I 3 210 LYS 210 210 210 LYS LYS A . n 
I 3 211 GLY 211 211 211 GLY GLY A . n 
I 3 212 ARG 212 212 212 ARG ARG A . n 
I 3 213 LEU 213 213 213 LEU LEU A . n 
I 3 214 PRO 214 214 214 PRO PRO A . n 
I 3 215 HIS 215 215 215 HIS HIS A . n 
I 3 216 ILE 216 216 216 ILE ILE A . n 
I 3 217 VAL 217 217 217 VAL VAL A . n 
I 3 218 VAL 218 218 218 VAL VAL A . n 
I 3 219 VAL 219 219 219 VAL VAL A . n 
I 3 220 THR 220 220 220 THR THR A . n 
I 3 221 ALA 221 221 221 ALA ALA A . n 
I 3 222 GLU 222 222 222 GLU GLU A . n 
I 3 223 PRO 223 223 223 PRO PRO A . n 
I 3 224 THR 224 224 224 THR THR A . n 
I 3 225 PRO 225 225 225 PRO PRO A . n 
I 3 226 SER 226 226 226 SER SER A . n 
I 3 227 ARG 227 227 227 ARG ARG A . n 
I 3 228 ILE 228 228 228 ILE ILE A . n 
I 3 229 SER 229 229 229 SER SER A . n 
I 3 230 SER 230 230 230 SER SER A . n 
I 3 231 ILE 231 231 231 ILE ILE A . n 
I 3 232 ALA 232 232 232 ALA ALA A . n 
I 3 233 LEU 233 233 233 LEU LEU A . n 
I 3 234 GLY 234 234 234 GLY GLY A . n 
I 3 235 THR 235 235 235 THR THR A . n 
I 3 236 GLY 236 236 236 GLY GLY A . n 
I 3 237 GLU 237 237 237 GLU GLU A . n 
I 3 238 ILE 238 238 238 ILE ILE A . n 
I 3 239 ASP 239 239 239 ASP ASP A . n 
I 3 240 CYS 240 240 240 CYS CYS A . n 
I 3 241 VAL 241 241 241 VAL VAL A . n 
I 3 242 TYR 242 242 242 TYR TYR A . n 
I 3 243 HIS 243 243 243 HIS HIS A . n 
I 3 244 PHE 244 244 244 PHE PHE A . n 
I 3 245 ALA 245 245 245 ALA ALA A . n 
I 3 246 LEU 246 246 246 LEU LEU A . n 
I 3 247 TYR 247 247 247 TYR TYR A . n 
I 3 248 GLU 248 248 248 GLU GLU A . n 
I 3 249 LEU 249 249 249 LEU LEU A . n 
I 3 250 GLU 250 250 250 GLU GLU A . n 
I 3 251 GLN 251 251 251 GLN GLN A . n 
I 3 252 ILE 252 252 252 ILE ILE A . n 
I 3 253 LEU 253 253 253 LEU LEU A . n 
I 3 254 GLN 254 254 254 GLN GLN A . n 
I 3 255 SER 255 255 255 SER SER A . n 
I 3 256 LEU 256 256 256 LEU LEU A . n 
I 3 257 ASN 257 257 257 ASN ASN A . n 
I 3 258 TYR 258 258 258 TYR TYR A . n 
I 3 259 GLU 259 259 259 GLU GLU A . n 
I 3 260 ASP 260 260 260 ASP ASP A . n 
I 3 261 ALA 261 261 261 ALA ALA A . n 
I 3 262 LEU 262 262 262 LEU LEU A . n 
I 3 263 ASP 263 263 263 ASP ASP A . n 
I 3 264 LEU 264 264 264 LEU LEU A . n 
I 3 265 PHE 265 265 265 PHE PHE A . n 
I 3 266 TYR 266 266 266 TYR TYR A . n 
I 3 267 ILE 267 267 267 ILE ILE A . n 
I 3 268 MET 268 268 268 MET MET A . n 
I 3 269 VAL 269 269 269 VAL VAL A . n 
I 3 270 ASN 270 270 270 ASN ASN A . n 
I 3 271 GLY 271 271 271 GLY GLY A . n 
I 3 272 LYS 272 272 272 LYS LYS A . n 
I 3 273 ARG 273 273 273 ARG ARG A . n 
I 3 274 LEU 274 274 274 LEU LEU A . n 
I 3 275 LYS 275 275 275 LYS LYS A . n 
I 3 276 ASP 276 276 276 ASP ASP A . n 
I 3 277 ILE 277 277 277 ILE ILE A . n 
I 3 278 SER 278 278 278 SER SER A . n 
I 3 279 ASP 279 279 279 ASP ASP A . n 
I 3 280 LEU 280 280 280 LEU LEU A . n 
I 3 281 PRO 281 281 281 PRO PRO A . n 
I 3 282 LEU 282 282 282 LEU LEU A . n 
I 3 283 ASP 283 283 283 ASP ASP A . n 
I 3 284 LEU 284 284 284 LEU LEU A . n 
I 3 285 ALA 285 285 285 ALA ALA A . n 
I 3 286 VAL 286 286 286 VAL VAL A . n 
J 3 1   MET 1   1   1   MET MET B . n 
J 3 2   GLN 2   2   2   GLN GLN B . n 
J 3 3   PRO 3   3   3   PRO PRO B . n 
J 3 4   LEU 4   4   4   LEU LEU B . n 
J 3 5   PHE 5   5   5   PHE PHE B . n 
J 3 6   THR 6   6   6   THR THR B . n 
J 3 7   GLN 7   7   7   GLN GLN B . n 
J 3 8   GLU 8   8   8   GLU GLU B . n 
J 3 9   ARG 9   9   9   ARG ARG B . n 
J 3 10  ARG 10  10  10  ARG ARG B . n 
J 3 11  ILE 11  11  11  ILE ILE B . n 
J 3 12  PHE 12  12  12  PHE PHE B . n 
J 3 13  HIS 13  13  13  HIS HIS B . n 
J 3 14  LYS 14  14  14  LYS LYS B . n 
J 3 15  LYS 15  15  15  LYS LYS B . n 
J 3 16  LEU 16  16  16  LEU LEU B . n 
J 3 17  LEU 17  17  17  LEU LEU B . n 
J 3 18  ASP 18  18  18  ASP ASP B . n 
J 3 19  GLY 19  19  19  GLY GLY B . n 
J 3 20  ASN 20  20  20  ASN ASN B . n 
J 3 21  ILE 21  21  21  ILE ILE B . n 
J 3 22  LEU 22  22  22  LEU LEU B . n 
J 3 23  ALA 23  23  23  ALA ALA B . n 
J 3 24  THR 24  24  24  THR THR B . n 
J 3 25  ASN 25  25  25  ASN ASN B . n 
J 3 26  ASN 26  26  26  ASN ASN B . n 
J 3 27  ARG 27  27  27  ARG ARG B . n 
J 3 28  GLY 28  28  28  GLY GLY B . n 
J 3 29  VAL 29  29  29  VAL VAL B . n 
J 3 30  VAL 30  30  30  VAL VAL B . n 
J 3 31  SER 31  31  31  SER SER B . n 
J 3 32  ASN 32  32  32  ASN ASN B . n 
J 3 33  ALA 33  33  33  ALA ALA B . n 
J 3 34  ASP 34  34  34  ASP ASP B . n 
J 3 35  GLY 35  35  35  GLY GLY B . n 
J 3 36  SER 36  36  36  SER SER B . n 
J 3 37  ASN 37  37  37  ASN ASN B . n 
J 3 38  THR 38  38  38  THR THR B . n 
J 3 39  ARG 39  39  39  ARG ARG B . n 
J 3 40  SER 40  40  40  SER SER B . n 
J 3 41  PHE 41  41  41  PHE PHE B . n 
J 3 42  ASN 42  42  42  ASN ASN B . n 
J 3 43  ILE 43  43  43  ILE ILE B . n 
J 3 44  ALA 44  44  44  ALA ALA B . n 
J 3 45  LYS 45  45  45  LYS LYS B . n 
J 3 46  GLY 46  46  46  GLY GLY B . n 
J 3 47  ILE 47  47  47  ILE ILE B . n 
J 3 48  ALA 48  48  48  ALA ALA B . n 
J 3 49  ASP 49  49  49  ASP ASP B . n 
J 3 50  LEU 50  50  50  LEU LEU B . n 
J 3 51  LEU 51  51  51  LEU LEU B . n 
J 3 52  HIS 52  52  52  HIS HIS B . n 
J 3 53  SER 53  53  53  SER SER B . n 
J 3 54  GLU 54  54  54  GLU GLU B . n 
J 3 55  THR 55  55  55  THR THR B . n 
J 3 56  VAL 56  56  56  VAL VAL B . n 
J 3 57  SER 57  57  57  SER SER B . n 
J 3 58  GLU 58  58  58  GLU GLU B . n 
J 3 59  ARG 59  59  59  ARG ARG B . n 
J 3 60  LEU 60  60  60  LEU LEU B . n 
J 3 61  PRO 61  61  61  PRO PRO B . n 
J 3 62  GLY 62  62  62  GLY GLY B . n 
J 3 63  GLN 63  63  63  GLN GLN B . n 
J 3 64  THR 64  64  64  THR THR B . n 
J 3 65  SER 65  65  65  SER SER B . n 
J 3 66  GLY 66  66  66  GLY GLY B . n 
J 3 67  ASN 67  67  67  ASN ASN B . n 
J 3 68  ALA 68  68  68  ALA ALA B . n 
J 3 69  PHE 69  69  69  PHE PHE B . n 
J 3 70  GLU 70  70  70  GLU GLU B . n 
J 3 71  ALA 71  71  71  ALA ALA B . n 
J 3 72  ILE 72  72  72  ILE ILE B . n 
J 3 73  CYS 73  73  73  CYS CYS B . n 
J 3 74  SER 74  74  74  SER SER B . n 
J 3 75  GLU 75  75  75  GLU GLU B . n 
J 3 76  PHE 76  76  76  PHE PHE B . n 
J 3 77  VAL 77  77  77  VAL VAL B . n 
J 3 78  GLN 78  78  78  GLN GLN B . n 
J 3 79  SER 79  79  79  SER SER B . n 
J 3 80  ALA 80  80  80  ALA ALA B . n 
J 3 81  PHE 81  81  81  PHE PHE B . n 
J 3 82  GLU 82  82  82  GLU GLU B . n 
J 3 83  LYS 83  83  83  LYS LYS B . n 
J 3 84  LEU 84  84  84  LEU LEU B . n 
J 3 85  GLN 85  85  85  GLN GLN B . n 
J 3 86  HIS 86  86  86  HIS HIS B . n 
J 3 87  ILE 87  87  87  ILE ILE B . n 
J 3 88  ARG 88  88  88  ARG ARG B . n 
J 3 89  PRO 89  89  89  PRO PRO B . n 
J 3 90  GLY 90  90  90  GLY GLY B . n 
J 3 91  ASP 91  91  91  ASP ASP B . n 
J 3 92  TRP 92  92  92  TRP TRP B . n 
J 3 93  ASN 93  93  93  ASN ASN B . n 
J 3 94  VAL 94  94  94  VAL VAL B . n 
J 3 95  LYS 95  95  95  LYS LYS B . n 
J 3 96  GLN 96  96  96  GLN GLN B . n 
J 3 97  VAL 97  97  97  VAL VAL B . n 
J 3 98  GLY 98  98  98  GLY GLY B . n 
J 3 99  SER 99  99  99  SER SER B . n 
J 3 100 ARG 100 100 100 ARG ARG B . n 
J 3 101 ASN 101 101 101 ASN ASN B . n 
J 3 102 ARG 102 102 102 ARG ARG B . n 
J 3 103 LEU 103 103 103 LEU LEU B . n 
J 3 104 GLU 104 104 104 GLU GLU B . n 
J 3 105 ILE 105 105 105 ILE ILE B . n 
J 3 106 ALA 106 106 106 ALA ALA B . n 
J 3 107 ARG 107 107 107 ARG ARG B . n 
J 3 108 TYR 108 108 108 TYR TYR B . n 
J 3 109 GLN 109 109 109 GLN GLN B . n 
J 3 110 GLN 110 110 110 GLN GLN B . n 
J 3 111 TYR 111 111 111 TYR TYR B . n 
J 3 112 ALA 112 112 112 ALA ALA B . n 
J 3 113 HIS 113 113 113 HIS HIS B . n 
J 3 114 LEU 114 114 114 LEU LEU B . n 
J 3 115 THR 115 115 115 THR THR B . n 
J 3 116 ALA 116 116 116 ALA ALA B . n 
J 3 117 LEU 117 117 117 LEU LEU B . n 
J 3 118 ALA 118 118 118 ALA ALA B . n 
J 3 119 LYS 119 119 119 LYS LYS B . n 
J 3 120 ALA 120 120 120 ALA ALA B . n 
J 3 121 ALA 121 121 121 ALA ALA B . n 
J 3 122 GLU 122 122 122 GLU GLU B . n 
J 3 123 GLU 123 123 123 GLU GLU B . n 
J 3 124 ASN 124 124 124 ASN ASN B . n 
J 3 125 PRO 125 125 125 PRO PRO B . n 
J 3 126 GLU 126 126 126 GLU GLU B . n 
J 3 127 LEU 127 127 127 LEU LEU B . n 
J 3 128 ALA 128 128 128 ALA ALA B . n 
J 3 129 ALA 129 129 129 ALA ALA B . n 
J 3 130 ALA 130 130 130 ALA ALA B . n 
J 3 131 LEU 131 131 131 LEU LEU B . n 
J 3 132 GLY 132 132 132 GLY GLY B . n 
J 3 133 SER 133 133 133 SER SER B . n 
J 3 134 ASP 134 134 134 ASP ASP B . n 
J 3 135 TYR 135 135 135 TYR TYR B . n 
J 3 136 THR 136 136 136 THR THR B . n 
J 3 137 ILE 137 137 137 ILE ILE B . n 
J 3 138 THR 138 138 138 THR THR B . n 
J 3 139 PRO 139 139 139 PRO PRO B . n 
J 3 140 ASP 140 140 140 ASP ASP B . n 
J 3 141 ILE 141 141 141 ILE ILE B . n 
J 3 142 ILE 142 142 142 ILE ILE B . n 
J 3 143 VAL 143 143 143 VAL VAL B . n 
J 3 144 THR 144 144 144 THR THR B . n 
J 3 145 ARG 145 145 145 ARG ARG B . n 
J 3 146 ASN 146 146 146 ASN ASN B . n 
J 3 147 LEU 147 147 147 LEU LEU B . n 
J 3 148 ILE 148 148 148 ILE ILE B . n 
J 3 149 ALA 149 149 149 ALA ALA B . n 
J 3 150 ASP 150 150 150 ASP ASP B . n 
J 3 151 ALA 151 151 151 ALA ALA B . n 
J 3 152 GLU 152 152 152 GLU GLU B . n 
J 3 153 ILE 153 153 153 ILE ILE B . n 
J 3 154 ASN 154 154 154 ASN ASN B . n 
J 3 155 ARG 155 155 155 ARG ARG B . n 
J 3 156 ASN 156 156 156 ASN ASN B . n 
J 3 157 GLU 157 157 157 GLU GLU B . n 
J 3 158 PHE 158 158 158 PHE PHE B . n 
J 3 159 LEU 159 159 159 LEU LEU B . n 
J 3 160 VAL 160 160 160 VAL VAL B . n 
J 3 161 ASP 161 161 161 ASP ASP B . n 
J 3 162 GLU 162 162 162 GLU GLU B . n 
J 3 163 ASN 163 163 163 ASN ASN B . n 
J 3 164 ILE 164 164 164 ILE ILE B . n 
J 3 165 ALA 165 165 165 ALA ALA B . n 
J 3 166 THR 166 166 166 THR THR B . n 
J 3 167 TYR 167 167 167 TYR TYR B . n 
J 3 168 ALA 168 168 168 ALA ALA B . n 
J 3 169 SER 169 169 169 SER SER B . n 
J 3 170 LEU 170 170 170 LEU LEU B . n 
J 3 171 ARG 171 171 171 ARG ARG B . n 
J 3 172 ALA 172 172 172 ALA ALA B . n 
J 3 173 GLY 173 173 173 GLY GLY B . n 
J 3 174 ASN 174 174 174 ASN ASN B . n 
J 3 175 GLY 175 175 175 GLY GLY B . n 
J 3 176 ASN 176 176 176 ASN ASN B . n 
J 3 177 MET 177 177 177 MET MET B . n 
J 3 178 PRO 178 178 178 PRO PRO B . n 
J 3 179 LEU 179 179 179 LEU LEU B . n 
J 3 180 LEU 180 180 180 LEU LEU B . n 
J 3 181 HIS 181 181 181 HIS HIS B . n 
J 3 182 ALA 182 182 182 ALA ALA B . n 
J 3 183 SER 183 183 183 SER SER B . n 
J 3 184 ILE 184 184 184 ILE ILE B . n 
J 3 185 SER 185 185 185 SER SER B . n 
J 3 186 CYS 186 186 186 CYS CYS B . n 
J 3 187 LYS 187 187 187 LYS LYS B . n 
J 3 188 TRP 188 188 188 TRP TRP B . n 
J 3 189 THR 189 189 189 THR THR B . n 
J 3 190 ILE 190 190 190 ILE ILE B . n 
J 3 191 ARG 191 191 191 ARG ARG B . n 
J 3 192 SER 192 192 192 SER SER B . n 
J 3 193 ASP 193 193 193 ASP ASP B . n 
J 3 194 ARG 194 194 194 ARG ARG B . n 
J 3 195 ALA 195 195 195 ALA ALA B . n 
J 3 196 GLN 196 196 196 GLN GLN B . n 
J 3 197 ASN 197 197 197 ASN ASN B . n 
J 3 198 ALA 198 198 198 ALA ALA B . n 
J 3 199 ARG 199 199 199 ARG ARG B . n 
J 3 200 SER 200 200 200 SER SER B . n 
J 3 201 GLU 201 201 201 GLU GLU B . n 
J 3 202 GLY 202 202 202 GLY GLY B . n 
J 3 203 LEU 203 203 203 LEU LEU B . n 
J 3 204 ASN 204 204 204 ASN ASN B . n 
J 3 205 LEU 205 205 205 LEU LEU B . n 
J 3 206 VAL 206 206 206 VAL VAL B . n 
J 3 207 ARG 207 207 207 ARG ARG B . n 
J 3 208 ASN 208 208 208 ASN ASN B . n 
J 3 209 ARG 209 209 209 ARG ARG B . n 
J 3 210 LYS 210 210 210 LYS LYS B . n 
J 3 211 GLY 211 211 211 GLY GLY B . n 
J 3 212 ARG 212 212 212 ARG ARG B . n 
J 3 213 LEU 213 213 213 LEU LEU B . n 
J 3 214 PRO 214 214 214 PRO PRO B . n 
J 3 215 HIS 215 215 215 HIS HIS B . n 
J 3 216 ILE 216 216 216 ILE ILE B . n 
J 3 217 VAL 217 217 217 VAL VAL B . n 
J 3 218 VAL 218 218 218 VAL VAL B . n 
J 3 219 VAL 219 219 219 VAL VAL B . n 
J 3 220 THR 220 220 220 THR THR B . n 
J 3 221 ALA 221 221 221 ALA ALA B . n 
J 3 222 GLU 222 222 222 GLU GLU B . n 
J 3 223 PRO 223 223 223 PRO PRO B . n 
J 3 224 THR 224 224 224 THR THR B . n 
J 3 225 PRO 225 225 225 PRO PRO B . n 
J 3 226 SER 226 226 226 SER SER B . n 
J 3 227 ARG 227 227 227 ARG ARG B . n 
J 3 228 ILE 228 228 228 ILE ILE B . n 
J 3 229 SER 229 229 229 SER SER B . n 
J 3 230 SER 230 230 230 SER SER B . n 
J 3 231 ILE 231 231 231 ILE ILE B . n 
J 3 232 ALA 232 232 232 ALA ALA B . n 
J 3 233 LEU 233 233 233 LEU LEU B . n 
J 3 234 GLY 234 234 234 GLY GLY B . n 
J 3 235 THR 235 235 235 THR THR B . n 
J 3 236 GLY 236 236 236 GLY GLY B . n 
J 3 237 GLU 237 237 237 GLU GLU B . n 
J 3 238 ILE 238 238 238 ILE ILE B . n 
J 3 239 ASP 239 239 239 ASP ASP B . n 
J 3 240 CYS 240 240 240 CYS CYS B . n 
J 3 241 VAL 241 241 241 VAL VAL B . n 
J 3 242 TYR 242 242 242 TYR TYR B . n 
J 3 243 HIS 243 243 243 HIS HIS B . n 
J 3 244 PHE 244 244 244 PHE PHE B . n 
J 3 245 ALA 245 245 245 ALA ALA B . n 
J 3 246 LEU 246 246 246 LEU LEU B . n 
J 3 247 TYR 247 247 247 TYR TYR B . n 
J 3 248 GLU 248 248 248 GLU GLU B . n 
J 3 249 LEU 249 249 249 LEU LEU B . n 
J 3 250 GLU 250 250 250 GLU GLU B . n 
J 3 251 GLN 251 251 251 GLN GLN B . n 
J 3 252 ILE 252 252 252 ILE ILE B . n 
J 3 253 LEU 253 253 253 LEU LEU B . n 
J 3 254 GLN 254 254 254 GLN GLN B . n 
J 3 255 SER 255 255 255 SER SER B . n 
J 3 256 LEU 256 256 256 LEU LEU B . n 
J 3 257 ASN 257 257 257 ASN ASN B . n 
J 3 258 TYR 258 258 258 TYR TYR B . n 
J 3 259 GLU 259 259 259 GLU GLU B . n 
J 3 260 ASP 260 260 260 ASP ASP B . n 
J 3 261 ALA 261 261 261 ALA ALA B . n 
J 3 262 LEU 262 262 262 LEU LEU B . n 
J 3 263 ASP 263 263 263 ASP ASP B . n 
J 3 264 LEU 264 264 264 LEU LEU B . n 
J 3 265 PHE 265 265 265 PHE PHE B . n 
J 3 266 TYR 266 266 266 TYR TYR B . n 
J 3 267 ILE 267 267 267 ILE ILE B . n 
J 3 268 MET 268 268 268 MET MET B . n 
J 3 269 VAL 269 269 269 VAL VAL B . n 
J 3 270 ASN 270 270 270 ASN ASN B . n 
J 3 271 GLY 271 271 271 GLY GLY B . n 
J 3 272 LYS 272 272 272 LYS LYS B . n 
J 3 273 ARG 273 273 273 ARG ARG B . n 
J 3 274 LEU 274 274 274 LEU LEU B . n 
J 3 275 LYS 275 275 275 LYS LYS B . n 
J 3 276 ASP 276 276 276 ASP ASP B . n 
J 3 277 ILE 277 277 277 ILE ILE B . n 
J 3 278 SER 278 278 278 SER SER B . n 
J 3 279 ASP 279 279 279 ASP ASP B . n 
J 3 280 LEU 280 280 280 LEU LEU B . n 
J 3 281 PRO 281 281 281 PRO PRO B . n 
J 3 282 LEU 282 282 282 LEU LEU B . n 
J 3 283 ASP 283 283 283 ASP ASP B . n 
J 3 284 LEU 284 284 284 LEU LEU B . n 
J 3 285 ALA 285 285 285 ALA ALA B . n 
J 3 286 VAL 286 286 286 VAL VAL B . n 
K 3 1   MET 1   1   1   MET MET C . n 
K 3 2   GLN 2   2   2   GLN GLN C . n 
K 3 3   PRO 3   3   3   PRO PRO C . n 
K 3 4   LEU 4   4   4   LEU LEU C . n 
K 3 5   PHE 5   5   5   PHE PHE C . n 
K 3 6   THR 6   6   6   THR THR C . n 
K 3 7   GLN 7   7   7   GLN GLN C . n 
K 3 8   GLU 8   8   8   GLU GLU C . n 
K 3 9   ARG 9   9   9   ARG ARG C . n 
K 3 10  ARG 10  10  10  ARG ARG C . n 
K 3 11  ILE 11  11  11  ILE ILE C . n 
K 3 12  PHE 12  12  12  PHE PHE C . n 
K 3 13  HIS 13  13  13  HIS HIS C . n 
K 3 14  LYS 14  14  14  LYS LYS C . n 
K 3 15  LYS 15  15  15  LYS LYS C . n 
K 3 16  LEU 16  16  16  LEU LEU C . n 
K 3 17  LEU 17  17  17  LEU LEU C . n 
K 3 18  ASP 18  18  18  ASP ASP C . n 
K 3 19  GLY 19  19  19  GLY GLY C . n 
K 3 20  ASN 20  20  20  ASN ASN C . n 
K 3 21  ILE 21  21  21  ILE ILE C . n 
K 3 22  LEU 22  22  22  LEU LEU C . n 
K 3 23  ALA 23  23  23  ALA ALA C . n 
K 3 24  THR 24  24  24  THR THR C . n 
K 3 25  ASN 25  25  25  ASN ASN C . n 
K 3 26  ASN 26  26  26  ASN ASN C . n 
K 3 27  ARG 27  27  27  ARG ARG C . n 
K 3 28  GLY 28  28  28  GLY GLY C . n 
K 3 29  VAL 29  29  29  VAL VAL C . n 
K 3 30  VAL 30  30  30  VAL VAL C . n 
K 3 31  SER 31  31  31  SER SER C . n 
K 3 32  ASN 32  32  32  ASN ASN C . n 
K 3 33  ALA 33  33  33  ALA ALA C . n 
K 3 34  ASP 34  34  34  ASP ASP C . n 
K 3 35  GLY 35  35  35  GLY GLY C . n 
K 3 36  SER 36  36  36  SER SER C . n 
K 3 37  ASN 37  37  37  ASN ASN C . n 
K 3 38  THR 38  38  38  THR THR C . n 
K 3 39  ARG 39  39  39  ARG ARG C . n 
K 3 40  SER 40  40  40  SER SER C . n 
K 3 41  PHE 41  41  41  PHE PHE C . n 
K 3 42  ASN 42  42  42  ASN ASN C . n 
K 3 43  ILE 43  43  43  ILE ILE C . n 
K 3 44  ALA 44  44  44  ALA ALA C . n 
K 3 45  LYS 45  45  45  LYS LYS C . n 
K 3 46  GLY 46  46  46  GLY GLY C . n 
K 3 47  ILE 47  47  47  ILE ILE C . n 
K 3 48  ALA 48  48  48  ALA ALA C . n 
K 3 49  ASP 49  49  49  ASP ASP C . n 
K 3 50  LEU 50  50  50  LEU LEU C . n 
K 3 51  LEU 51  51  51  LEU LEU C . n 
K 3 52  HIS 52  52  52  HIS HIS C . n 
K 3 53  SER 53  53  53  SER SER C . n 
K 3 54  GLU 54  54  54  GLU GLU C . n 
K 3 55  THR 55  55  55  THR THR C . n 
K 3 56  VAL 56  56  56  VAL VAL C . n 
K 3 57  SER 57  57  57  SER SER C . n 
K 3 58  GLU 58  58  58  GLU GLU C . n 
K 3 59  ARG 59  59  59  ARG ARG C . n 
K 3 60  LEU 60  60  60  LEU LEU C . n 
K 3 61  PRO 61  61  61  PRO PRO C . n 
K 3 62  GLY 62  62  62  GLY GLY C . n 
K 3 63  GLN 63  63  63  GLN GLN C . n 
K 3 64  THR 64  64  64  THR THR C . n 
K 3 65  SER 65  65  65  SER SER C . n 
K 3 66  GLY 66  66  66  GLY GLY C . n 
K 3 67  ASN 67  67  67  ASN ASN C . n 
K 3 68  ALA 68  68  68  ALA ALA C . n 
K 3 69  PHE 69  69  69  PHE PHE C . n 
K 3 70  GLU 70  70  70  GLU GLU C . n 
K 3 71  ALA 71  71  71  ALA ALA C . n 
K 3 72  ILE 72  72  72  ILE ILE C . n 
K 3 73  CYS 73  73  73  CYS CYS C . n 
K 3 74  SER 74  74  74  SER SER C . n 
K 3 75  GLU 75  75  75  GLU GLU C . n 
K 3 76  PHE 76  76  76  PHE PHE C . n 
K 3 77  VAL 77  77  77  VAL VAL C . n 
K 3 78  GLN 78  78  78  GLN GLN C . n 
K 3 79  SER 79  79  79  SER SER C . n 
K 3 80  ALA 80  80  80  ALA ALA C . n 
K 3 81  PHE 81  81  81  PHE PHE C . n 
K 3 82  GLU 82  82  82  GLU GLU C . n 
K 3 83  LYS 83  83  83  LYS LYS C . n 
K 3 84  LEU 84  84  84  LEU LEU C . n 
K 3 85  GLN 85  85  85  GLN GLN C . n 
K 3 86  HIS 86  86  86  HIS HIS C . n 
K 3 87  ILE 87  87  87  ILE ILE C . n 
K 3 88  ARG 88  88  88  ARG ARG C . n 
K 3 89  PRO 89  89  89  PRO PRO C . n 
K 3 90  GLY 90  90  90  GLY GLY C . n 
K 3 91  ASP 91  91  91  ASP ASP C . n 
K 3 92  TRP 92  92  92  TRP TRP C . n 
K 3 93  ASN 93  93  93  ASN ASN C . n 
K 3 94  VAL 94  94  94  VAL VAL C . n 
K 3 95  LYS 95  95  95  LYS LYS C . n 
K 3 96  GLN 96  96  96  GLN GLN C . n 
K 3 97  VAL 97  97  97  VAL VAL C . n 
K 3 98  GLY 98  98  98  GLY GLY C . n 
K 3 99  SER 99  99  99  SER SER C . n 
K 3 100 ARG 100 100 100 ARG ARG C . n 
K 3 101 ASN 101 101 101 ASN ASN C . n 
K 3 102 ARG 102 102 102 ARG ARG C . n 
K 3 103 LEU 103 103 103 LEU LEU C . n 
K 3 104 GLU 104 104 104 GLU GLU C . n 
K 3 105 ILE 105 105 105 ILE ILE C . n 
K 3 106 ALA 106 106 106 ALA ALA C . n 
K 3 107 ARG 107 107 107 ARG ARG C . n 
K 3 108 TYR 108 108 108 TYR TYR C . n 
K 3 109 GLN 109 109 109 GLN GLN C . n 
K 3 110 GLN 110 110 110 GLN GLN C . n 
K 3 111 TYR 111 111 111 TYR TYR C . n 
K 3 112 ALA 112 112 112 ALA ALA C . n 
K 3 113 HIS 113 113 113 HIS HIS C . n 
K 3 114 LEU 114 114 114 LEU LEU C . n 
K 3 115 THR 115 115 115 THR THR C . n 
K 3 116 ALA 116 116 116 ALA ALA C . n 
K 3 117 LEU 117 117 117 LEU LEU C . n 
K 3 118 ALA 118 118 118 ALA ALA C . n 
K 3 119 LYS 119 119 119 LYS LYS C . n 
K 3 120 ALA 120 120 120 ALA ALA C . n 
K 3 121 ALA 121 121 121 ALA ALA C . n 
K 3 122 GLU 122 122 122 GLU GLU C . n 
K 3 123 GLU 123 123 123 GLU GLU C . n 
K 3 124 ASN 124 124 124 ASN ASN C . n 
K 3 125 PRO 125 125 125 PRO PRO C . n 
K 3 126 GLU 126 126 126 GLU GLU C . n 
K 3 127 LEU 127 127 127 LEU LEU C . n 
K 3 128 ALA 128 128 128 ALA ALA C . n 
K 3 129 ALA 129 129 129 ALA ALA C . n 
K 3 130 ALA 130 130 130 ALA ALA C . n 
K 3 131 LEU 131 131 131 LEU LEU C . n 
K 3 132 GLY 132 132 132 GLY GLY C . n 
K 3 133 SER 133 133 133 SER SER C . n 
K 3 134 ASP 134 134 134 ASP ASP C . n 
K 3 135 TYR 135 135 135 TYR TYR C . n 
K 3 136 THR 136 136 136 THR THR C . n 
K 3 137 ILE 137 137 137 ILE ILE C . n 
K 3 138 THR 138 138 138 THR THR C . n 
K 3 139 PRO 139 139 139 PRO PRO C . n 
K 3 140 ASP 140 140 140 ASP ASP C . n 
K 3 141 ILE 141 141 141 ILE ILE C . n 
K 3 142 ILE 142 142 142 ILE ILE C . n 
K 3 143 VAL 143 143 143 VAL VAL C . n 
K 3 144 THR 144 144 144 THR THR C . n 
K 3 145 ARG 145 145 145 ARG ARG C . n 
K 3 146 ASN 146 146 146 ASN ASN C . n 
K 3 147 LEU 147 147 147 LEU LEU C . n 
K 3 148 ILE 148 148 148 ILE ILE C . n 
K 3 149 ALA 149 149 149 ALA ALA C . n 
K 3 150 ASP 150 150 150 ASP ASP C . n 
K 3 151 ALA 151 151 151 ALA ALA C . n 
K 3 152 GLU 152 152 152 GLU GLU C . n 
K 3 153 ILE 153 153 153 ILE ILE C . n 
K 3 154 ASN 154 154 154 ASN ASN C . n 
K 3 155 ARG 155 155 155 ARG ARG C . n 
K 3 156 ASN 156 156 156 ASN ASN C . n 
K 3 157 GLU 157 157 157 GLU GLU C . n 
K 3 158 PHE 158 158 158 PHE PHE C . n 
K 3 159 LEU 159 159 159 LEU LEU C . n 
K 3 160 VAL 160 160 160 VAL VAL C . n 
K 3 161 ASP 161 161 161 ASP ASP C . n 
K 3 162 GLU 162 162 162 GLU GLU C . n 
K 3 163 ASN 163 163 163 ASN ASN C . n 
K 3 164 ILE 164 164 164 ILE ILE C . n 
K 3 165 ALA 165 165 165 ALA ALA C . n 
K 3 166 THR 166 166 166 THR THR C . n 
K 3 167 TYR 167 167 167 TYR TYR C . n 
K 3 168 ALA 168 168 168 ALA ALA C . n 
K 3 169 SER 169 169 169 SER SER C . n 
K 3 170 LEU 170 170 170 LEU LEU C . n 
K 3 171 ARG 171 171 171 ARG ARG C . n 
K 3 172 ALA 172 172 172 ALA ALA C . n 
K 3 173 GLY 173 173 173 GLY GLY C . n 
K 3 174 ASN 174 174 174 ASN ASN C . n 
K 3 175 GLY 175 175 175 GLY GLY C . n 
K 3 176 ASN 176 176 176 ASN ASN C . n 
K 3 177 MET 177 177 177 MET MET C . n 
K 3 178 PRO 178 178 178 PRO PRO C . n 
K 3 179 LEU 179 179 179 LEU LEU C . n 
K 3 180 LEU 180 180 180 LEU LEU C . n 
K 3 181 HIS 181 181 181 HIS HIS C . n 
K 3 182 ALA 182 182 182 ALA ALA C . n 
K 3 183 SER 183 183 183 SER SER C . n 
K 3 184 ILE 184 184 184 ILE ILE C . n 
K 3 185 SER 185 185 185 SER SER C . n 
K 3 186 CYS 186 186 186 CYS CYS C . n 
K 3 187 LYS 187 187 187 LYS LYS C . n 
K 3 188 TRP 188 188 188 TRP TRP C . n 
K 3 189 THR 189 189 189 THR THR C . n 
K 3 190 ILE 190 190 190 ILE ILE C . n 
K 3 191 ARG 191 191 191 ARG ARG C . n 
K 3 192 SER 192 192 192 SER SER C . n 
K 3 193 ASP 193 193 193 ASP ASP C . n 
K 3 194 ARG 194 194 194 ARG ARG C . n 
K 3 195 ALA 195 195 195 ALA ALA C . n 
K 3 196 GLN 196 196 196 GLN GLN C . n 
K 3 197 ASN 197 197 197 ASN ASN C . n 
K 3 198 ALA 198 198 198 ALA ALA C . n 
K 3 199 ARG 199 199 199 ARG ARG C . n 
K 3 200 SER 200 200 200 SER SER C . n 
K 3 201 GLU 201 201 201 GLU GLU C . n 
K 3 202 GLY 202 202 202 GLY GLY C . n 
K 3 203 LEU 203 203 203 LEU LEU C . n 
K 3 204 ASN 204 204 204 ASN ASN C . n 
K 3 205 LEU 205 205 205 LEU LEU C . n 
K 3 206 VAL 206 206 206 VAL VAL C . n 
K 3 207 ARG 207 207 207 ARG ARG C . n 
K 3 208 ASN 208 208 208 ASN ASN C . n 
K 3 209 ARG 209 209 209 ARG ARG C . n 
K 3 210 LYS 210 210 210 LYS LYS C . n 
K 3 211 GLY 211 211 211 GLY GLY C . n 
K 3 212 ARG 212 212 212 ARG ARG C . n 
K 3 213 LEU 213 213 213 LEU LEU C . n 
K 3 214 PRO 214 214 214 PRO PRO C . n 
K 3 215 HIS 215 215 215 HIS HIS C . n 
K 3 216 ILE 216 216 216 ILE ILE C . n 
K 3 217 VAL 217 217 217 VAL VAL C . n 
K 3 218 VAL 218 218 218 VAL VAL C . n 
K 3 219 VAL 219 219 219 VAL VAL C . n 
K 3 220 THR 220 220 220 THR THR C . n 
K 3 221 ALA 221 221 221 ALA ALA C . n 
K 3 222 GLU 222 222 222 GLU GLU C . n 
K 3 223 PRO 223 223 223 PRO PRO C . n 
K 3 224 THR 224 224 224 THR THR C . n 
K 3 225 PRO 225 225 225 PRO PRO C . n 
K 3 226 SER 226 226 226 SER SER C . n 
K 3 227 ARG 227 227 227 ARG ARG C . n 
K 3 228 ILE 228 228 228 ILE ILE C . n 
K 3 229 SER 229 229 229 SER SER C . n 
K 3 230 SER 230 230 230 SER SER C . n 
K 3 231 ILE 231 231 231 ILE ILE C . n 
K 3 232 ALA 232 232 232 ALA ALA C . n 
K 3 233 LEU 233 233 233 LEU LEU C . n 
K 3 234 GLY 234 234 234 GLY GLY C . n 
K 3 235 THR 235 235 235 THR THR C . n 
K 3 236 GLY 236 236 236 GLY GLY C . n 
K 3 237 GLU 237 237 237 GLU GLU C . n 
K 3 238 ILE 238 238 238 ILE ILE C . n 
K 3 239 ASP 239 239 239 ASP ASP C . n 
K 3 240 CYS 240 240 240 CYS CYS C . n 
K 3 241 VAL 241 241 241 VAL VAL C . n 
K 3 242 TYR 242 242 242 TYR TYR C . n 
K 3 243 HIS 243 243 243 HIS HIS C . n 
K 3 244 PHE 244 244 244 PHE PHE C . n 
K 3 245 ALA 245 245 245 ALA ALA C . n 
K 3 246 LEU 246 246 246 LEU LEU C . n 
K 3 247 TYR 247 247 247 TYR TYR C . n 
K 3 248 GLU 248 248 248 GLU GLU C . n 
K 3 249 LEU 249 249 249 LEU LEU C . n 
K 3 250 GLU 250 250 250 GLU GLU C . n 
K 3 251 GLN 251 251 251 GLN GLN C . n 
K 3 252 ILE 252 252 252 ILE ILE C . n 
K 3 253 LEU 253 253 253 LEU LEU C . n 
K 3 254 GLN 254 254 254 GLN GLN C . n 
K 3 255 SER 255 255 255 SER SER C . n 
K 3 256 LEU 256 256 256 LEU LEU C . n 
K 3 257 ASN 257 257 257 ASN ASN C . n 
K 3 258 TYR 258 258 258 TYR TYR C . n 
K 3 259 GLU 259 259 259 GLU GLU C . n 
K 3 260 ASP 260 260 260 ASP ASP C . n 
K 3 261 ALA 261 261 261 ALA ALA C . n 
K 3 262 LEU 262 262 262 LEU LEU C . n 
K 3 263 ASP 263 263 263 ASP ASP C . n 
K 3 264 LEU 264 264 264 LEU LEU C . n 
K 3 265 PHE 265 265 265 PHE PHE C . n 
K 3 266 TYR 266 266 266 TYR TYR C . n 
K 3 267 ILE 267 267 267 ILE ILE C . n 
K 3 268 MET 268 268 268 MET MET C . n 
K 3 269 VAL 269 269 269 VAL VAL C . n 
K 3 270 ASN 270 270 270 ASN ASN C . n 
K 3 271 GLY 271 271 271 GLY GLY C . n 
K 3 272 LYS 272 272 272 LYS LYS C . n 
K 3 273 ARG 273 273 273 ARG ARG C . n 
K 3 274 LEU 274 274 274 LEU LEU C . n 
K 3 275 LYS 275 275 275 LYS LYS C . n 
K 3 276 ASP 276 276 276 ASP ASP C . n 
K 3 277 ILE 277 277 277 ILE ILE C . n 
K 3 278 SER 278 278 278 SER SER C . n 
K 3 279 ASP 279 279 279 ASP ASP C . n 
K 3 280 LEU 280 280 280 LEU LEU C . n 
K 3 281 PRO 281 281 281 PRO PRO C . n 
K 3 282 LEU 282 282 282 LEU LEU C . n 
K 3 283 ASP 283 283 283 ASP ASP C . n 
K 3 284 LEU 284 284 284 LEU LEU C . n 
K 3 285 ALA 285 285 285 ALA ALA C . n 
K 3 286 VAL 286 286 286 VAL VAL C . n 
L 3 1   MET 1   1   1   MET MET D . n 
L 3 2   GLN 2   2   2   GLN GLN D . n 
L 3 3   PRO 3   3   3   PRO PRO D . n 
L 3 4   LEU 4   4   4   LEU LEU D . n 
L 3 5   PHE 5   5   5   PHE PHE D . n 
L 3 6   THR 6   6   6   THR THR D . n 
L 3 7   GLN 7   7   7   GLN GLN D . n 
L 3 8   GLU 8   8   8   GLU GLU D . n 
L 3 9   ARG 9   9   9   ARG ARG D . n 
L 3 10  ARG 10  10  10  ARG ARG D . n 
L 3 11  ILE 11  11  11  ILE ILE D . n 
L 3 12  PHE 12  12  12  PHE PHE D . n 
L 3 13  HIS 13  13  13  HIS HIS D . n 
L 3 14  LYS 14  14  14  LYS LYS D . n 
L 3 15  LYS 15  15  15  LYS LYS D . n 
L 3 16  LEU 16  16  16  LEU LEU D . n 
L 3 17  LEU 17  17  17  LEU LEU D . n 
L 3 18  ASP 18  18  18  ASP ASP D . n 
L 3 19  GLY 19  19  19  GLY GLY D . n 
L 3 20  ASN 20  20  20  ASN ASN D . n 
L 3 21  ILE 21  21  21  ILE ILE D . n 
L 3 22  LEU 22  22  22  LEU LEU D . n 
L 3 23  ALA 23  23  23  ALA ALA D . n 
L 3 24  THR 24  24  24  THR THR D . n 
L 3 25  ASN 25  25  25  ASN ASN D . n 
L 3 26  ASN 26  26  26  ASN ASN D . n 
L 3 27  ARG 27  27  27  ARG ARG D . n 
L 3 28  GLY 28  28  28  GLY GLY D . n 
L 3 29  VAL 29  29  29  VAL VAL D . n 
L 3 30  VAL 30  30  30  VAL VAL D . n 
L 3 31  SER 31  31  31  SER SER D . n 
L 3 32  ASN 32  32  32  ASN ASN D . n 
L 3 33  ALA 33  33  33  ALA ALA D . n 
L 3 34  ASP 34  34  34  ASP ASP D . n 
L 3 35  GLY 35  35  35  GLY GLY D . n 
L 3 36  SER 36  36  36  SER SER D . n 
L 3 37  ASN 37  37  37  ASN ASN D . n 
L 3 38  THR 38  38  38  THR THR D . n 
L 3 39  ARG 39  39  39  ARG ARG D . n 
L 3 40  SER 40  40  40  SER SER D . n 
L 3 41  PHE 41  41  41  PHE PHE D . n 
L 3 42  ASN 42  42  42  ASN ASN D . n 
L 3 43  ILE 43  43  43  ILE ILE D . n 
L 3 44  ALA 44  44  44  ALA ALA D . n 
L 3 45  LYS 45  45  45  LYS LYS D . n 
L 3 46  GLY 46  46  46  GLY GLY D . n 
L 3 47  ILE 47  47  47  ILE ILE D . n 
L 3 48  ALA 48  48  48  ALA ALA D . n 
L 3 49  ASP 49  49  49  ASP ASP D . n 
L 3 50  LEU 50  50  50  LEU LEU D . n 
L 3 51  LEU 51  51  51  LEU LEU D . n 
L 3 52  HIS 52  52  52  HIS HIS D . n 
L 3 53  SER 53  53  53  SER SER D . n 
L 3 54  GLU 54  54  54  GLU GLU D . n 
L 3 55  THR 55  55  55  THR THR D . n 
L 3 56  VAL 56  56  56  VAL VAL D . n 
L 3 57  SER 57  57  57  SER SER D . n 
L 3 58  GLU 58  58  58  GLU GLU D . n 
L 3 59  ARG 59  59  59  ARG ARG D . n 
L 3 60  LEU 60  60  60  LEU LEU D . n 
L 3 61  PRO 61  61  61  PRO PRO D . n 
L 3 62  GLY 62  62  62  GLY GLY D . n 
L 3 63  GLN 63  63  63  GLN GLN D . n 
L 3 64  THR 64  64  64  THR THR D . n 
L 3 65  SER 65  65  65  SER SER D . n 
L 3 66  GLY 66  66  66  GLY GLY D . n 
L 3 67  ASN 67  67  67  ASN ASN D . n 
L 3 68  ALA 68  68  68  ALA ALA D . n 
L 3 69  PHE 69  69  69  PHE PHE D . n 
L 3 70  GLU 70  70  70  GLU GLU D . n 
L 3 71  ALA 71  71  71  ALA ALA D . n 
L 3 72  ILE 72  72  72  ILE ILE D . n 
L 3 73  CYS 73  73  73  CYS CYS D . n 
L 3 74  SER 74  74  74  SER SER D . n 
L 3 75  GLU 75  75  75  GLU GLU D . n 
L 3 76  PHE 76  76  76  PHE PHE D . n 
L 3 77  VAL 77  77  77  VAL VAL D . n 
L 3 78  GLN 78  78  78  GLN GLN D . n 
L 3 79  SER 79  79  79  SER SER D . n 
L 3 80  ALA 80  80  80  ALA ALA D . n 
L 3 81  PHE 81  81  81  PHE PHE D . n 
L 3 82  GLU 82  82  82  GLU GLU D . n 
L 3 83  LYS 83  83  83  LYS LYS D . n 
L 3 84  LEU 84  84  84  LEU LEU D . n 
L 3 85  GLN 85  85  85  GLN GLN D . n 
L 3 86  HIS 86  86  86  HIS HIS D . n 
L 3 87  ILE 87  87  87  ILE ILE D . n 
L 3 88  ARG 88  88  88  ARG ARG D . n 
L 3 89  PRO 89  89  89  PRO PRO D . n 
L 3 90  GLY 90  90  90  GLY GLY D . n 
L 3 91  ASP 91  91  91  ASP ASP D . n 
L 3 92  TRP 92  92  92  TRP TRP D . n 
L 3 93  ASN 93  93  93  ASN ASN D . n 
L 3 94  VAL 94  94  94  VAL VAL D . n 
L 3 95  LYS 95  95  95  LYS LYS D . n 
L 3 96  GLN 96  96  96  GLN GLN D . n 
L 3 97  VAL 97  97  97  VAL VAL D . n 
L 3 98  GLY 98  98  98  GLY GLY D . n 
L 3 99  SER 99  99  99  SER SER D . n 
L 3 100 ARG 100 100 100 ARG ARG D . n 
L 3 101 ASN 101 101 101 ASN ASN D . n 
L 3 102 ARG 102 102 102 ARG ARG D . n 
L 3 103 LEU 103 103 103 LEU LEU D . n 
L 3 104 GLU 104 104 104 GLU GLU D . n 
L 3 105 ILE 105 105 105 ILE ILE D . n 
L 3 106 ALA 106 106 106 ALA ALA D . n 
L 3 107 ARG 107 107 107 ARG ARG D . n 
L 3 108 TYR 108 108 108 TYR TYR D . n 
L 3 109 GLN 109 109 109 GLN GLN D . n 
L 3 110 GLN 110 110 110 GLN GLN D . n 
L 3 111 TYR 111 111 111 TYR TYR D . n 
L 3 112 ALA 112 112 112 ALA ALA D . n 
L 3 113 HIS 113 113 113 HIS HIS D . n 
L 3 114 LEU 114 114 114 LEU LEU D . n 
L 3 115 THR 115 115 115 THR THR D . n 
L 3 116 ALA 116 116 116 ALA ALA D . n 
L 3 117 LEU 117 117 117 LEU LEU D . n 
L 3 118 ALA 118 118 118 ALA ALA D . n 
L 3 119 LYS 119 119 119 LYS LYS D . n 
L 3 120 ALA 120 120 120 ALA ALA D . n 
L 3 121 ALA 121 121 121 ALA ALA D . n 
L 3 122 GLU 122 122 122 GLU GLU D . n 
L 3 123 GLU 123 123 123 GLU GLU D . n 
L 3 124 ASN 124 124 124 ASN ASN D . n 
L 3 125 PRO 125 125 125 PRO PRO D . n 
L 3 126 GLU 126 126 126 GLU GLU D . n 
L 3 127 LEU 127 127 127 LEU LEU D . n 
L 3 128 ALA 128 128 128 ALA ALA D . n 
L 3 129 ALA 129 129 129 ALA ALA D . n 
L 3 130 ALA 130 130 130 ALA ALA D . n 
L 3 131 LEU 131 131 131 LEU LEU D . n 
L 3 132 GLY 132 132 132 GLY GLY D . n 
L 3 133 SER 133 133 133 SER SER D . n 
L 3 134 ASP 134 134 134 ASP ASP D . n 
L 3 135 TYR 135 135 135 TYR TYR D . n 
L 3 136 THR 136 136 136 THR THR D . n 
L 3 137 ILE 137 137 137 ILE ILE D . n 
L 3 138 THR 138 138 138 THR THR D . n 
L 3 139 PRO 139 139 139 PRO PRO D . n 
L 3 140 ASP 140 140 140 ASP ASP D . n 
L 3 141 ILE 141 141 141 ILE ILE D . n 
L 3 142 ILE 142 142 142 ILE ILE D . n 
L 3 143 VAL 143 143 143 VAL VAL D . n 
L 3 144 THR 144 144 144 THR THR D . n 
L 3 145 ARG 145 145 145 ARG ARG D . n 
L 3 146 ASN 146 146 146 ASN ASN D . n 
L 3 147 LEU 147 147 147 LEU LEU D . n 
L 3 148 ILE 148 148 148 ILE ILE D . n 
L 3 149 ALA 149 149 149 ALA ALA D . n 
L 3 150 ASP 150 150 150 ASP ASP D . n 
L 3 151 ALA 151 151 151 ALA ALA D . n 
L 3 152 GLU 152 152 152 GLU GLU D . n 
L 3 153 ILE 153 153 153 ILE ILE D . n 
L 3 154 ASN 154 154 154 ASN ASN D . n 
L 3 155 ARG 155 155 155 ARG ARG D . n 
L 3 156 ASN 156 156 156 ASN ASN D . n 
L 3 157 GLU 157 157 157 GLU GLU D . n 
L 3 158 PHE 158 158 158 PHE PHE D . n 
L 3 159 LEU 159 159 159 LEU LEU D . n 
L 3 160 VAL 160 160 160 VAL VAL D . n 
L 3 161 ASP 161 161 161 ASP ASP D . n 
L 3 162 GLU 162 162 162 GLU GLU D . n 
L 3 163 ASN 163 163 163 ASN ASN D . n 
L 3 164 ILE 164 164 164 ILE ILE D . n 
L 3 165 ALA 165 165 165 ALA ALA D . n 
L 3 166 THR 166 166 166 THR THR D . n 
L 3 167 TYR 167 167 167 TYR TYR D . n 
L 3 168 ALA 168 168 168 ALA ALA D . n 
L 3 169 SER 169 169 169 SER SER D . n 
L 3 170 LEU 170 170 170 LEU LEU D . n 
L 3 171 ARG 171 171 171 ARG ARG D . n 
L 3 172 ALA 172 172 172 ALA ALA D . n 
L 3 173 GLY 173 173 173 GLY GLY D . n 
L 3 174 ASN 174 174 174 ASN ASN D . n 
L 3 175 GLY 175 175 175 GLY GLY D . n 
L 3 176 ASN 176 176 176 ASN ASN D . n 
L 3 177 MET 177 177 177 MET MET D . n 
L 3 178 PRO 178 178 178 PRO PRO D . n 
L 3 179 LEU 179 179 179 LEU LEU D . n 
L 3 180 LEU 180 180 180 LEU LEU D . n 
L 3 181 HIS 181 181 181 HIS HIS D . n 
L 3 182 ALA 182 182 182 ALA ALA D . n 
L 3 183 SER 183 183 183 SER SER D . n 
L 3 184 ILE 184 184 184 ILE ILE D . n 
L 3 185 SER 185 185 185 SER SER D . n 
L 3 186 CYS 186 186 186 CYS CYS D . n 
L 3 187 LYS 187 187 187 LYS LYS D . n 
L 3 188 TRP 188 188 188 TRP TRP D . n 
L 3 189 THR 189 189 189 THR THR D . n 
L 3 190 ILE 190 190 190 ILE ILE D . n 
L 3 191 ARG 191 191 191 ARG ARG D . n 
L 3 192 SER 192 192 192 SER SER D . n 
L 3 193 ASP 193 193 193 ASP ASP D . n 
L 3 194 ARG 194 194 194 ARG ARG D . n 
L 3 195 ALA 195 195 195 ALA ALA D . n 
L 3 196 GLN 196 196 196 GLN GLN D . n 
L 3 197 ASN 197 197 197 ASN ASN D . n 
L 3 198 ALA 198 198 198 ALA ALA D . n 
L 3 199 ARG 199 199 199 ARG ARG D . n 
L 3 200 SER 200 200 200 SER SER D . n 
L 3 201 GLU 201 201 201 GLU GLU D . n 
L 3 202 GLY 202 202 202 GLY GLY D . n 
L 3 203 LEU 203 203 203 LEU LEU D . n 
L 3 204 ASN 204 204 204 ASN ASN D . n 
L 3 205 LEU 205 205 205 LEU LEU D . n 
L 3 206 VAL 206 206 206 VAL VAL D . n 
L 3 207 ARG 207 207 207 ARG ARG D . n 
L 3 208 ASN 208 208 208 ASN ASN D . n 
L 3 209 ARG 209 209 209 ARG ARG D . n 
L 3 210 LYS 210 210 210 LYS LYS D . n 
L 3 211 GLY 211 211 211 GLY GLY D . n 
L 3 212 ARG 212 212 212 ARG ARG D . n 
L 3 213 LEU 213 213 213 LEU LEU D . n 
L 3 214 PRO 214 214 214 PRO PRO D . n 
L 3 215 HIS 215 215 215 HIS HIS D . n 
L 3 216 ILE 216 216 216 ILE ILE D . n 
L 3 217 VAL 217 217 217 VAL VAL D . n 
L 3 218 VAL 218 218 218 VAL VAL D . n 
L 3 219 VAL 219 219 219 VAL VAL D . n 
L 3 220 THR 220 220 220 THR THR D . n 
L 3 221 ALA 221 221 221 ALA ALA D . n 
L 3 222 GLU 222 222 222 GLU GLU D . n 
L 3 223 PRO 223 223 223 PRO PRO D . n 
L 3 224 THR 224 224 224 THR THR D . n 
L 3 225 PRO 225 225 225 PRO PRO D . n 
L 3 226 SER 226 226 226 SER SER D . n 
L 3 227 ARG 227 227 227 ARG ARG D . n 
L 3 228 ILE 228 228 228 ILE ILE D . n 
L 3 229 SER 229 229 229 SER SER D . n 
L 3 230 SER 230 230 230 SER SER D . n 
L 3 231 ILE 231 231 231 ILE ILE D . n 
L 3 232 ALA 232 232 232 ALA ALA D . n 
L 3 233 LEU 233 233 233 LEU LEU D . n 
L 3 234 GLY 234 234 234 GLY GLY D . n 
L 3 235 THR 235 235 235 THR THR D . n 
L 3 236 GLY 236 236 236 GLY GLY D . n 
L 3 237 GLU 237 237 237 GLU GLU D . n 
L 3 238 ILE 238 238 238 ILE ILE D . n 
L 3 239 ASP 239 239 239 ASP ASP D . n 
L 3 240 CYS 240 240 240 CYS CYS D . n 
L 3 241 VAL 241 241 241 VAL VAL D . n 
L 3 242 TYR 242 242 242 TYR TYR D . n 
L 3 243 HIS 243 243 243 HIS HIS D . n 
L 3 244 PHE 244 244 244 PHE PHE D . n 
L 3 245 ALA 245 245 245 ALA ALA D . n 
L 3 246 LEU 246 246 246 LEU LEU D . n 
L 3 247 TYR 247 247 247 TYR TYR D . n 
L 3 248 GLU 248 248 248 GLU GLU D . n 
L 3 249 LEU 249 249 249 LEU LEU D . n 
L 3 250 GLU 250 250 250 GLU GLU D . n 
L 3 251 GLN 251 251 251 GLN GLN D . n 
L 3 252 ILE 252 252 252 ILE ILE D . n 
L 3 253 LEU 253 253 253 LEU LEU D . n 
L 3 254 GLN 254 254 254 GLN GLN D . n 
L 3 255 SER 255 255 255 SER SER D . n 
L 3 256 LEU 256 256 256 LEU LEU D . n 
L 3 257 ASN 257 257 257 ASN ASN D . n 
L 3 258 TYR 258 258 258 TYR TYR D . n 
L 3 259 GLU 259 259 259 GLU GLU D . n 
L 3 260 ASP 260 260 260 ASP ASP D . n 
L 3 261 ALA 261 261 261 ALA ALA D . n 
L 3 262 LEU 262 262 262 LEU LEU D . n 
L 3 263 ASP 263 263 263 ASP ASP D . n 
L 3 264 LEU 264 264 264 LEU LEU D . n 
L 3 265 PHE 265 265 265 PHE PHE D . n 
L 3 266 TYR 266 266 266 TYR TYR D . n 
L 3 267 ILE 267 267 267 ILE ILE D . n 
L 3 268 MET 268 268 268 MET MET D . n 
L 3 269 VAL 269 269 269 VAL VAL D . n 
L 3 270 ASN 270 270 270 ASN ASN D . n 
L 3 271 GLY 271 271 271 GLY GLY D . n 
L 3 272 LYS 272 272 272 LYS LYS D . n 
L 3 273 ARG 273 273 273 ARG ARG D . n 
L 3 274 LEU 274 274 274 LEU LEU D . n 
L 3 275 LYS 275 275 275 LYS LYS D . n 
L 3 276 ASP 276 276 276 ASP ASP D . n 
L 3 277 ILE 277 277 277 ILE ILE D . n 
L 3 278 SER 278 278 278 SER SER D . n 
L 3 279 ASP 279 279 279 ASP ASP D . n 
L 3 280 LEU 280 280 280 LEU LEU D . n 
L 3 281 PRO 281 281 281 PRO PRO D . n 
L 3 282 LEU 282 282 282 LEU LEU D . n 
L 3 283 ASP 283 283 283 ASP ASP D . n 
L 3 284 LEU 284 284 284 LEU LEU D . n 
L 3 285 ALA 285 285 285 ALA ALA D . n 
L 3 286 VAL 286 286 286 VAL VAL D . n 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dodecameric 
_pdbx_struct_assembly.oligomeric_count     12 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   OP2 ? D  DC  1   ? J DC  5    ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 O   ? I  CYS 186 ? A CYS 186  ? 1_555 164.6 ? 
2   OP2 ? D  DC  1   ? J DC  5    ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 O   ? R  ACY .   ? A ACY 2001 ? 1_555 94.3  ? 
3   O   ? I  CYS 186 ? A CYS 186  ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 O   ? R  ACY .   ? A ACY 2001 ? 1_555 94.0  ? 
4   OP2 ? D  DC  1   ? J DC  5    ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 O   ? BA HOH .   ? J HOH 221  ? 1_555 85.3  ? 
5   O   ? I  CYS 186 ? A CYS 186  ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 O   ? BA HOH .   ? J HOH 221  ? 1_555 82.9  ? 
6   O   ? R  ACY .   ? A ACY 2001 ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 O   ? BA HOH .   ? J HOH 221  ? 1_555 82.4  ? 
7   OP2 ? D  DC  1   ? J DC  5    ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 O   ? GA HOH .   ? A HOH 5564 ? 1_555 92.7  ? 
8   O   ? I  CYS 186 ? A CYS 186  ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 O   ? GA HOH .   ? A HOH 5564 ? 1_555 79.4  ? 
9   O   ? R  ACY .   ? A ACY 2001 ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 O   ? GA HOH .   ? A HOH 5564 ? 1_555 173.0 ? 
10  O   ? BA HOH .   ? J HOH 221  ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 O   ? GA HOH .   ? A HOH 5564 ? 1_555 99.0  ? 
11  OP2 ? D  DC  1   ? J DC  5    ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 OD2 ? I  ASP 140 ? A ASP 140  ? 1_555 101.4 ? 
12  O   ? I  CYS 186 ? A CYS 186  ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 OD2 ? I  ASP 140 ? A ASP 140  ? 1_555 91.3  ? 
13  O   ? R  ACY .   ? A ACY 2001 ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 OD2 ? I  ASP 140 ? A ASP 140  ? 1_555 91.8  ? 
14  O   ? BA HOH .   ? J HOH 221  ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 OD2 ? I  ASP 140 ? A ASP 140  ? 1_555 171.4 ? 
15  O   ? GA HOH .   ? A HOH 5564 ? 1_555 MG ? Q MG . ? A MG 5555 ? 1_555 OD2 ? I  ASP 140 ? A ASP 140  ? 1_555 86.1  ? 
16  OD2 ? J  ASP 140 ? B ASP 140  ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 OP2 ? B  DC  1   ? I DC  5    ? 1_555 101.2 ? 
17  OD2 ? J  ASP 140 ? B ASP 140  ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? J  CYS 186 ? B CYS 186  ? 1_555 91.9  ? 
18  OP2 ? B  DC  1   ? I DC  5    ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? J  CYS 186 ? B CYS 186  ? 1_555 164.0 ? 
19  OD2 ? J  ASP 140 ? B ASP 140  ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 OXT ? T  ACY .   ? B ACY 3002 ? 1_555 92.5  ? 
20  OP2 ? B  DC  1   ? I DC  5    ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 OXT ? T  ACY .   ? B ACY 3002 ? 1_555 97.0  ? 
21  O   ? J  CYS 186 ? B CYS 186  ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 OXT ? T  ACY .   ? B ACY 3002 ? 1_555 91.5  ? 
22  OD2 ? J  ASP 140 ? B ASP 140  ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? Z  HOH .   ? I HOH 57   ? 1_555 172.1 ? 
23  OP2 ? B  DC  1   ? I DC  5    ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? Z  HOH .   ? I HOH 57   ? 1_555 86.4  ? 
24  O   ? J  CYS 186 ? B CYS 186  ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? Z  HOH .   ? I HOH 57   ? 1_555 80.9  ? 
25  OXT ? T  ACY .   ? B ACY 3002 ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? Z  HOH .   ? I HOH 57   ? 1_555 84.3  ? 
26  OD2 ? J  ASP 140 ? B ASP 140  ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? HA HOH .   ? B HOH 3390 ? 1_555 83.5  ? 
27  OP2 ? B  DC  1   ? I DC  5    ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? HA HOH .   ? B HOH 3390 ? 1_555 92.1  ? 
28  O   ? J  CYS 186 ? B CYS 186  ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? HA HOH .   ? B HOH 3390 ? 1_555 80.2  ? 
29  OXT ? T  ACY .   ? B ACY 3002 ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? HA HOH .   ? B HOH 3390 ? 1_555 170.6 ? 
30  O   ? Z  HOH .   ? I HOH 57   ? 1_555 MG ? S MG . ? B MG 3333 ? 1_555 O   ? HA HOH .   ? B HOH 3390 ? 1_555 98.6  ? 
31  O   ? V  ACY .   ? C ACY 4003 ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 OP2 ? F  DC  1   ? K DC  5    ? 1_555 91.6  ? 
32  O   ? V  ACY .   ? C ACY 4003 ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 O   ? IA HOH .   ? C HOH 7781 ? 1_555 175.2 ? 
33  OP2 ? F  DC  1   ? K DC  5    ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 O   ? IA HOH .   ? C HOH 7781 ? 1_555 93.0  ? 
34  O   ? V  ACY .   ? C ACY 4003 ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 O   ? K  CYS 186 ? C CYS 186  ? 1_555 94.0  ? 
35  OP2 ? F  DC  1   ? K DC  5    ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 O   ? K  CYS 186 ? C CYS 186  ? 1_555 164.8 ? 
36  O   ? IA HOH .   ? C HOH 7781 ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 O   ? K  CYS 186 ? C CYS 186  ? 1_555 82.0  ? 
37  O   ? V  ACY .   ? C ACY 4003 ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 OD2 ? K  ASP 140 ? C ASP 140  ? 1_555 92.9  ? 
38  OP2 ? F  DC  1   ? K DC  5    ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 OD2 ? K  ASP 140 ? C ASP 140  ? 1_555 101.2 ? 
39  O   ? IA HOH .   ? C HOH 7781 ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 OD2 ? K  ASP 140 ? C ASP 140  ? 1_555 84.9  ? 
40  O   ? K  CYS 186 ? C CYS 186  ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 OD2 ? K  ASP 140 ? C ASP 140  ? 1_555 92.7  ? 
41  O   ? V  ACY .   ? C ACY 4003 ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 O   ? DA HOH .   ? K HOH 328  ? 1_555 82.9  ? 
42  OP2 ? F  DC  1   ? K DC  5    ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 O   ? DA HOH .   ? K HOH 328  ? 1_555 83.3  ? 
43  O   ? IA HOH .   ? C HOH 7781 ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 O   ? DA HOH .   ? K HOH 328  ? 1_555 99.0  ? 
44  O   ? K  CYS 186 ? C CYS 186  ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 O   ? DA HOH .   ? K HOH 328  ? 1_555 83.4  ? 
45  OD2 ? K  ASP 140 ? C ASP 140  ? 1_555 MG ? U MG . ? C MG 7777 ? 1_555 O   ? DA HOH .   ? K HOH 328  ? 1_555 174.0 ? 
46  O   ? L  CYS 186 ? D CYS 186  ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 OD2 ? L  ASP 140 ? D ASP 140  ? 1_555 91.6  ? 
47  O   ? L  CYS 186 ? D CYS 186  ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 O   ? FA HOH .   ? L HOH 55   ? 1_555 82.1  ? 
48  OD2 ? L  ASP 140 ? D ASP 140  ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 O   ? FA HOH .   ? L HOH 55   ? 1_555 172.7 ? 
49  O   ? L  CYS 186 ? D CYS 186  ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 OXT ? X  ACY .   ? D ACY 5004 ? 1_555 92.9  ? 
50  OD2 ? L  ASP 140 ? D ASP 140  ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 OXT ? X  ACY .   ? D ACY 5004 ? 1_555 96.2  ? 
51  O   ? FA HOH .   ? L HOH 55   ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 OXT ? X  ACY .   ? D ACY 5004 ? 1_555 80.7  ? 
52  O   ? L  CYS 186 ? D CYS 186  ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 OP2 ? H  DC  1   ? L DC  5    ? 1_555 164.7 ? 
53  OD2 ? L  ASP 140 ? D ASP 140  ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 OP2 ? H  DC  1   ? L DC  5    ? 1_555 100.8 ? 
54  O   ? FA HOH .   ? L HOH 55   ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 OP2 ? H  DC  1   ? L DC  5    ? 1_555 86.1  ? 
55  OXT ? X  ACY .   ? D ACY 5004 ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 OP2 ? H  DC  1   ? L DC  5    ? 1_555 94.6  ? 
56  O   ? L  CYS 186 ? D CYS 186  ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 O   ? JA HOH .   ? D HOH 1022 ? 1_555 79.1  ? 
57  OD2 ? L  ASP 140 ? D ASP 140  ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 O   ? JA HOH .   ? D HOH 1022 ? 1_555 82.6  ? 
58  O   ? FA HOH .   ? L HOH 55   ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 O   ? JA HOH .   ? D HOH 1022 ? 1_555 99.6  ? 
59  OXT ? X  ACY .   ? D ACY 5004 ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 O   ? JA HOH .   ? D HOH 1022 ? 1_555 171.9 ? 
60  OP2 ? H  DC  1   ? L DC  5    ? 1_555 MG ? W MG . ? D MG 9999 ? 1_555 O   ? JA HOH .   ? D HOH 1022 ? 1_555 93.5  ? 
61  OP3 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 OP2 ? B  DC  1   ? I DC  5    ? 1_555 53.5  ? 
62  OP3 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 OD1 ? J  ASP 140 ? B ASP 140  ? 1_555 136.5 ? 
63  OP2 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 OD1 ? J  ASP 140 ? B ASP 140  ? 1_555 92.1  ? 
64  OP3 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? Z  HOH .   ? I HOH 259  ? 1_555 55.3  ? 
65  OP2 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? Z  HOH .   ? I HOH 259  ? 1_555 99.6  ? 
66  OD1 ? J  ASP 140 ? B ASP 140  ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? Z  HOH .   ? I HOH 259  ? 1_555 167.7 ? 
67  OP3 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? HA HOH .   ? B HOH 3345 ? 1_555 74.1  ? 
68  OP2 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? HA HOH .   ? B HOH 3345 ? 1_555 97.8  ? 
69  OD1 ? J  ASP 140 ? B ASP 140  ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? HA HOH .   ? B HOH 3345 ? 1_555 87.5  ? 
70  O   ? Z  HOH .   ? I HOH 259  ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? HA HOH .   ? B HOH 3345 ? 1_555 94.6  ? 
71  OP3 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? HA HOH .   ? B HOH 3403 ? 1_555 130.0 ? 
72  OP2 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? HA HOH .   ? B HOH 3403 ? 1_555 166.9 ? 
73  OD1 ? J  ASP 140 ? B ASP 140  ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? HA HOH .   ? B HOH 3403 ? 1_555 89.9  ? 
74  O   ? Z  HOH .   ? I HOH 259  ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? HA HOH .   ? B HOH 3403 ? 1_555 77.9  ? 
75  O   ? HA HOH .   ? B HOH 3345 ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? HA HOH .   ? B HOH 3403 ? 1_555 95.3  ? 
76  OP3 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? T  ACY .   ? B ACY 3002 ? 1_555 106.7 ? 
77  OP2 ? B  DC  1   ? I DC  5    ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? T  ACY .   ? B ACY 3002 ? 1_555 83.5  ? 
78  OD1 ? J  ASP 140 ? B ASP 140  ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? T  ACY .   ? B ACY 3002 ? 1_555 92.5  ? 
79  O   ? Z  HOH .   ? I HOH 259  ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? T  ACY .   ? B ACY 3002 ? 1_555 85.2  ? 
80  O   ? HA HOH .   ? B HOH 3345 ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? T  ACY .   ? B ACY 3002 ? 1_555 178.8 ? 
81  O   ? HA HOH .   ? B HOH 3403 ? 1_555 MG ? M MG . ? I MG 2222 ? 1_555 O   ? T  ACY .   ? B ACY 3002 ? 1_555 83.5  ? 
82  OXT ? R  ACY .   ? A ACY 2001 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 O   ? GA HOH .   ? A HOH 5562 ? 1_555 84.2  ? 
83  OXT ? R  ACY .   ? A ACY 2001 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 O   ? AA HOH .   ? F HOH 22   ? 1_555 176.1 ? 
84  O   ? GA HOH .   ? A HOH 5562 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 O   ? AA HOH .   ? F HOH 22   ? 1_555 92.8  ? 
85  OXT ? R  ACY .   ? A ACY 2001 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OP3 ? D  DC  1   ? J DC  5    ? 1_555 104.5 ? 
86  O   ? GA HOH .   ? A HOH 5562 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OP3 ? D  DC  1   ? J DC  5    ? 1_555 59.2  ? 
87  O   ? AA HOH .   ? F HOH 22   ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OP3 ? D  DC  1   ? J DC  5    ? 1_555 75.9  ? 
88  OXT ? R  ACY .   ? A ACY 2001 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OP2 ? D  DC  1   ? J DC  5    ? 1_555 81.9  ? 
89  O   ? GA HOH .   ? A HOH 5562 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OP2 ? D  DC  1   ? J DC  5    ? 1_555 107.4 ? 
90  O   ? AA HOH .   ? F HOH 22   ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OP2 ? D  DC  1   ? J DC  5    ? 1_555 101.5 ? 
91  OP3 ? D  DC  1   ? J DC  5    ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OP2 ? D  DC  1   ? J DC  5    ? 1_555 56.7  ? 
92  OXT ? R  ACY .   ? A ACY 2001 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OD1 ? I  ASP 140 ? A ASP 140  ? 1_555 93.1  ? 
93  O   ? GA HOH .   ? A HOH 5562 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OD1 ? I  ASP 140 ? A ASP 140  ? 1_555 163.9 ? 
94  O   ? AA HOH .   ? F HOH 22   ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OD1 ? I  ASP 140 ? A ASP 140  ? 1_555 89.1  ? 
95  OP3 ? D  DC  1   ? J DC  5    ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OD1 ? I  ASP 140 ? A ASP 140  ? 1_555 136.5 ? 
96  OP2 ? D  DC  1   ? J DC  5    ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 OD1 ? I  ASP 140 ? A ASP 140  ? 1_555 87.9  ? 
97  OXT ? R  ACY .   ? A ACY 2001 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 O   ? GA HOH .   ? A HOH 5593 ? 1_555 78.2  ? 
98  O   ? GA HOH .   ? A HOH 5562 ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 O   ? GA HOH .   ? A HOH 5593 ? 1_555 73.5  ? 
99  O   ? AA HOH .   ? F HOH 22   ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 O   ? GA HOH .   ? A HOH 5593 ? 1_555 98.5  ? 
100 OP3 ? D  DC  1   ? J DC  5    ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 O   ? GA HOH .   ? A HOH 5593 ? 1_555 131.7 ? 
101 OP2 ? D  DC  1   ? J DC  5    ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 O   ? GA HOH .   ? A HOH 5593 ? 1_555 159.9 ? 
102 OD1 ? I  ASP 140 ? A ASP 140  ? 1_555 MG ? N MG . ? J MG 4444 ? 1_555 O   ? GA HOH .   ? A HOH 5593 ? 1_555 90.4  ? 
103 OP3 ? F  DC  1   ? K DC  5    ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 OXT ? V  ACY .   ? C ACY 4003 ? 1_555 108.1 ? 
104 OP3 ? F  DC  1   ? K DC  5    ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 OP2 ? F  DC  1   ? K DC  5    ? 1_555 55.5  ? 
105 OXT ? V  ACY .   ? C ACY 4003 ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 OP2 ? F  DC  1   ? K DC  5    ? 1_555 83.1  ? 
106 OP3 ? F  DC  1   ? K DC  5    ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? IA HOH .   ? C HOH 7780 ? 1_555 131.7 ? 
107 OXT ? V  ACY .   ? C ACY 4003 ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? IA HOH .   ? C HOH 7780 ? 1_555 80.1  ? 
108 OP2 ? F  DC  1   ? K DC  5    ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? IA HOH .   ? C HOH 7780 ? 1_555 163.1 ? 
109 OP3 ? F  DC  1   ? K DC  5    ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? DA HOH .   ? K HOH 271  ? 1_555 55.0  ? 
110 OXT ? V  ACY .   ? C ACY 4003 ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? DA HOH .   ? K HOH 271  ? 1_555 86.7  ? 
111 OP2 ? F  DC  1   ? K DC  5    ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? DA HOH .   ? K HOH 271  ? 1_555 101.2 ? 
112 O   ? IA HOH .   ? C HOH 7780 ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? DA HOH .   ? K HOH 271  ? 1_555 78.9  ? 
113 OP3 ? F  DC  1   ? K DC  5    ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? IA HOH .   ? C HOH 7779 ? 1_555 77.9  ? 
114 OXT ? V  ACY .   ? C ACY 4003 ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? IA HOH .   ? C HOH 7779 ? 1_555 171.4 ? 
115 OP2 ? F  DC  1   ? K DC  5    ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? IA HOH .   ? C HOH 7779 ? 1_555 105.5 ? 
116 O   ? IA HOH .   ? C HOH 7780 ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? IA HOH .   ? C HOH 7779 ? 1_555 91.4  ? 
117 O   ? DA HOH .   ? K HOH 271  ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 O   ? IA HOH .   ? C HOH 7779 ? 1_555 92.0  ? 
118 OP3 ? F  DC  1   ? K DC  5    ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 OD1 ? K  ASP 140 ? C ASP 140  ? 1_555 134.1 ? 
119 OXT ? V  ACY .   ? C ACY 4003 ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 OD1 ? K  ASP 140 ? C ASP 140  ? 1_555 91.8  ? 
120 OP2 ? F  DC  1   ? K DC  5    ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 OD1 ? K  ASP 140 ? C ASP 140  ? 1_555 87.9  ? 
121 O   ? IA HOH .   ? C HOH 7780 ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 OD1 ? K  ASP 140 ? C ASP 140  ? 1_555 91.6  ? 
122 O   ? DA HOH .   ? K HOH 271  ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 OD1 ? K  ASP 140 ? C ASP 140  ? 1_555 170.5 ? 
123 O   ? IA HOH .   ? C HOH 7779 ? 1_555 MG ? O MG . ? K MG 6666 ? 1_555 OD1 ? K  ASP 140 ? C ASP 140  ? 1_555 88.1  ? 
124 OD1 ? L  ASP 140 ? D ASP 140  ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 OP3 ? H  DC  1   ? L DC  5    ? 1_555 131.5 ? 
125 OD1 ? L  ASP 140 ? D ASP 140  ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? X  ACY .   ? D ACY 5004 ? 1_555 91.3  ? 
126 OP3 ? H  DC  1   ? L DC  5    ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? X  ACY .   ? D ACY 5004 ? 1_555 114.8 ? 
127 OD1 ? L  ASP 140 ? D ASP 140  ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 OP2 ? H  DC  1   ? L DC  5    ? 1_555 90.1  ? 
128 OP3 ? H  DC  1   ? L DC  5    ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 OP2 ? H  DC  1   ? L DC  5    ? 1_555 54.1  ? 
129 O   ? X  ACY .   ? D ACY 5004 ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 OP2 ? H  DC  1   ? L DC  5    ? 1_555 86.9  ? 
130 OD1 ? L  ASP 140 ? D ASP 140  ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1109 ? 1_555 169.3 ? 
131 OP3 ? H  DC  1   ? L DC  5    ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1109 ? 1_555 58.7  ? 
132 O   ? X  ACY .   ? D ACY 5004 ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1109 ? 1_555 85.8  ? 
133 OP2 ? H  DC  1   ? L DC  5    ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1109 ? 1_555 100.1 ? 
134 OD1 ? L  ASP 140 ? D ASP 140  ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1026 ? 1_555 87.7  ? 
135 OP3 ? H  DC  1   ? L DC  5    ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1026 ? 1_555 133.2 ? 
136 O   ? X  ACY .   ? D ACY 5004 ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1026 ? 1_555 83.1  ? 
137 OP2 ? H  DC  1   ? L DC  5    ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1026 ? 1_555 169.7 ? 
138 O   ? JA HOH .   ? D HOH 1109 ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1026 ? 1_555 81.6  ? 
139 OD1 ? L  ASP 140 ? D ASP 140  ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1118 ? 1_555 88.6  ? 
140 OP3 ? H  DC  1   ? L DC  5    ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1118 ? 1_555 72.5  ? 
141 O   ? X  ACY .   ? D ACY 5004 ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1118 ? 1_555 169.6 ? 
142 OP2 ? H  DC  1   ? L DC  5    ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1118 ? 1_555 103.5 ? 
143 O   ? JA HOH .   ? D HOH 1109 ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1118 ? 1_555 92.4  ? 
144 O   ? JA HOH .   ? D HOH 1026 ? 1_555 MG ? P MG . ? L MG 8888 ? 1_555 O   ? JA HOH .   ? D HOH 1118 ? 1_555 86.5  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2001-02-07 
2 'Structure model' 1 1 2008-04-27 
3 'Structure model' 1 2 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
SHARP     phasing          . ? 1 
X-PLOR    refinement       . ? 2 
DENZO     'data reduction' . ? 3 
SCALEPACK 'data scaling'   . ? 4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   C GLU 126  ? ? N   C ALA 128  ? ? 1.95 
2  1 O   C ALA 129  ? ? O   C HOH 8027 ? ? 1.97 
3  1 OE1 B GLN 85   ? ? O   B HOH 3476 ? ? 2.03 
4  1 O   K HOH 300  ? ? O   L HOH 458  ? ? 2.04 
5  1 O   K HOH 459  ? ? O   L HOH 460  ? ? 2.05 
6  1 O   D HOH 1056 ? ? O   D HOH 1173 ? ? 2.06 
7  1 N   D GLY 234  ? ? O   C HOH 8027 ? ? 2.07 
8  1 O   I HOH 411  ? ? O   A HOH 5635 ? ? 2.08 
9  1 O   J HOH 268  ? ? O   A HOH 5635 ? ? 2.09 
10 1 O   D HOH 1044 ? ? O   D HOH 1173 ? ? 2.10 
11 1 O   I HOH 411  ? ? O   J HOH 389  ? ? 2.10 
12 1 O   K HOH 459  ? ? O   L HOH 458  ? ? 2.10 
13 1 O   I HOH 266  ? ? O   B HOH 3605 ? ? 2.10 
14 1 OD2 C ASP 134  ? ? ND2 C ASN 204  ? ? 2.11 
15 1 O   H HOH 817  ? ? O   C HOH 7988 ? ? 2.13 
16 1 O   C ALA 121  ? ? O   C ASN 124  ? ? 2.14 
17 1 O   C GLU 126  ? ? N   C ALA 129  ? ? 2.15 
18 1 OD1 A ASN 124  ? ? O   A HOH 5732 ? ? 2.15 
19 1 O   B VAL 97   ? ? O   B HOH 3556 ? ? 2.15 
20 1 O   I HOH 677  ? ? O   I HOH 1279 ? ? 2.16 
21 1 O   J HOH 268  ? ? O   J HOH 412  ? ? 2.16 
22 1 O   I HOH 414  ? ? O   J HOH 268  ? ? 2.17 
23 1 O   B HOH 3347 ? ? O   B HOH 3451 ? ? 2.17 
24 1 O   K HOH 313  ? ? O   C HOH 8017 ? ? 2.18 
25 1 NH2 B ARG 145  ? ? O   B HOH 3543 ? ? 2.18 
26 1 O   D HOH 1123 ? ? O   D HOH 1147 ? ? 2.18 
27 1 O   L HOH 302  ? ? O   L HOH 460  ? ? 2.18 
28 1 O   E HOH 434  ? ? O   A HOH 5639 ? ? 2.19 
29 1 O   K HOH 828  ? ? O   L HOH 458  ? ? 2.19 
30 1 O   D HOH 1171 ? ? O   D HOH 1297 ? ? 2.19 
31 1 O   A HOH 5721 ? ? O   A HOH 5726 ? ? 2.19 
32 1 O   A HOH 5666 ? ? O   A HOH 5809 ? ? 2.19 
33 1 O   L HOH 275  ? ? O   D HOH 1299 ? ? 2.19 
34 1 O   E HOH 434  ? ? O   J HOH 435  ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 P I DC 5 ? ? OP3 I DC 5 ? ? 1.514 1.607 -0.093 0.012 N 
2 1 P J DC 5 ? ? OP3 J DC 5 ? ? 1.510 1.607 -0.097 0.012 N 
3 1 P K DC 5 ? ? OP3 K DC 5 ? ? 1.531 1.607 -0.076 0.012 N 
4 1 P L DC 5 ? ? OP3 L DC 5 ? ? 1.525 1.607 -0.082 0.012 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C A ASN 124 ? ? N A PRO 125 ? ? CA A PRO 125 ? ? 130.38 119.30 11.08 1.50 Y 
2 1 C C ASN 124 ? ? N C PRO 125 ? ? CA C PRO 125 ? ? 128.89 119.30 9.59  1.50 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 88  ? ? -153.11 72.53   
2  1 SER A 99  ? ? -44.11  -16.87  
3  1 GLU A 122 ? ? -64.33  16.18   
4  1 PRO A 125 ? ? -36.77  -88.83  
5  1 GLU A 126 ? ? -63.73  1.74    
6  1 SER A 133 ? ? -142.28 -5.50   
7  1 TYR A 135 ? ? -54.37  -9.52   
8  1 ASN A 174 ? ? -63.12  14.45   
9  1 ALA A 245 ? ? -155.58 63.92   
10 1 ARG B 88  ? ? -151.54 74.05   
11 1 SER B 99  ? ? -58.02  -9.81   
12 1 ARG B 100 ? ? -80.10  35.21   
13 1 ASN B 101 ? ? -165.20 83.78   
14 1 ASN B 124 ? ? -119.59 62.29   
15 1 GLU B 126 ? ? 112.82  -47.15  
16 1 SER B 133 ? ? -146.09 -24.18  
17 1 ALA B 172 ? ? -68.85  78.00   
18 1 ASN B 174 ? ? -52.84  51.21   
19 1 ALA B 245 ? ? -157.07 65.23   
20 1 ARG C 88  ? ? -152.93 72.84   
21 1 ASN C 101 ? ? -73.17  -71.01  
22 1 PRO C 125 ? ? -47.46  -113.28 
23 1 LEU C 127 ? ? 8.01    -53.56  
24 1 THR C 136 ? ? -72.44  33.24   
25 1 ILE C 137 ? ? -25.53  137.69  
26 1 ASN C 174 ? ? -35.02  121.14  
27 1 ALA C 245 ? ? -154.00 64.38   
28 1 ARG D 88  ? ? -152.39 78.41   
29 1 VAL D 97  ? ? -124.33 -78.51  
30 1 ASN D 101 ? ? -172.83 136.92  
31 1 ASN D 174 ? ? -111.97 56.59   
32 1 ALA D 245 ? ? -152.41 62.99   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1  1 DG  E 2   ? ? 0.079 'SIDE CHAIN' 
2  1 DG  E 4   ? ? 0.063 'SIDE CHAIN' 
3  1 DG  I 10  ? ? 0.079 'SIDE CHAIN' 
4  1 DG  F 2   ? ? 0.078 'SIDE CHAIN' 
5  1 DG  F 4   ? ? 0.064 'SIDE CHAIN' 
6  1 DG  J 10  ? ? 0.083 'SIDE CHAIN' 
7  1 DG  K 10  ? ? 0.066 'SIDE CHAIN' 
8  1 DG  H 2   ? ? 0.070 'SIDE CHAIN' 
9  1 DC  H 3   ? ? 0.064 'SIDE CHAIN' 
10 1 DG  H 4   ? ? 0.067 'SIDE CHAIN' 
11 1 DG  L 10  ? ? 0.071 'SIDE CHAIN' 
12 1 TYR A 108 ? ? 0.072 'SIDE CHAIN' 
13 1 TYR B 108 ? ? 0.063 'SIDE CHAIN' 
14 1 TYR C 108 ? ? 0.074 'SIDE CHAIN' 
15 1 TYR D 108 ? ? 0.073 'SIDE CHAIN' 
# 
loop_
_ndb_struct_conf_na.entry_id 
_ndb_struct_conf_na.feature 
1FIU 'double helix'        
1FIU 'b-form double helix' 
# 
loop_
_ndb_struct_na_base_pair.model_number 
_ndb_struct_na_base_pair.i_label_asym_id 
_ndb_struct_na_base_pair.i_label_comp_id 
_ndb_struct_na_base_pair.i_label_seq_id 
_ndb_struct_na_base_pair.i_symmetry 
_ndb_struct_na_base_pair.j_label_asym_id 
_ndb_struct_na_base_pair.j_label_comp_id 
_ndb_struct_na_base_pair.j_label_seq_id 
_ndb_struct_na_base_pair.j_symmetry 
_ndb_struct_na_base_pair.shear 
_ndb_struct_na_base_pair.stretch 
_ndb_struct_na_base_pair.stagger 
_ndb_struct_na_base_pair.buckle 
_ndb_struct_na_base_pair.propeller 
_ndb_struct_na_base_pair.opening 
_ndb_struct_na_base_pair.pair_number 
_ndb_struct_na_base_pair.pair_name 
_ndb_struct_na_base_pair.i_auth_asym_id 
_ndb_struct_na_base_pair.i_auth_seq_id 
_ndb_struct_na_base_pair.i_PDB_ins_code 
_ndb_struct_na_base_pair.j_auth_asym_id 
_ndb_struct_na_base_pair.j_auth_seq_id 
_ndb_struct_na_base_pair.j_PDB_ins_code 
_ndb_struct_na_base_pair.hbond_type_28 
_ndb_struct_na_base_pair.hbond_type_12 
1 A DG 2 1_555 D DC 7 1_555 -0.484 -0.191 0.116  2.201   -17.757 4.534  1  E_DG2:DC11_J E 2  ? J 11 ? 19 1 
1 A DC 3 1_555 D DG 6 1_555 0.158  -0.183 0.508  -2.111  -11.470 -1.757 2  E_DC3:DG10_J E 3  ? J 10 ? 19 1 
1 A DG 4 1_555 D DC 5 1_555 -0.240 -0.121 0.032  -2.216  -2.868  -1.303 3  E_DG4:DC9_J  E 4  ? J 9  ? 19 1 
1 B DC 1 1_555 D DG 4 1_555 0.282  -0.069 0.401  -10.787 -16.573 1.094  4  I_DC5:DG8_J  I 5  ? J 8  ? 19 1 
1 B DC 2 1_555 D DG 3 1_555 -0.016 -0.034 0.164  -11.082 11.337  -0.537 5  I_DC6:DG7_J  I 6  ? J 7  ? 19 1 
1 B DG 3 1_555 D DC 2 1_555 0.100  0.038  0.129  10.274  9.281   0.223  6  I_DG7:DC6_J  I 7  ? J 6  ? 19 1 
1 B DG 4 1_555 D DC 1 1_555 -0.247 -0.111 0.360  8.804   -16.682 0.887  7  I_DG8:DC5_J  I 8  ? J 5  ? 19 1 
1 B DC 5 1_555 C DG 4 1_555 0.228  -0.164 0.077  -0.273  0.713   -1.722 8  I_DC9:DG4_F  I 9  ? F 4  ? 19 1 
1 B DG 6 1_555 C DC 3 1_555 -0.137 -0.174 0.270  1.879   -12.846 -1.866 9  I_DG10:DC3_F I 10 ? F 3  ? 19 1 
1 B DC 7 1_555 C DG 2 1_555 -0.745 0.134  0.311  2.184   -9.721  -4.134 10 I_DC11:DG2_F I 11 ? F 2  ? 19 1 
1 E DG 2 1_555 H DC 7 1_555 0.019  -0.129 0.217  3.284   -8.673  -6.372 11 G_DG2:DC11_L G 2  ? L 11 ? 19 1 
1 E DC 3 1_555 H DG 6 1_555 -0.030 -0.197 0.405  -3.450  -20.537 -8.987 12 G_DC3:DG10_L G 3  ? L 10 ? 19 1 
1 E DG 4 1_555 H DC 5 1_555 -0.199 -0.148 -0.029 -4.167  0.236   -3.027 13 G_DG4:DC9_L  G 4  ? L 9  ? 19 1 
1 F DC 1 1_555 H DG 4 1_555 0.212  -0.142 0.302  -9.495  -14.787 0.725  14 K_DC5:DG8_L  K 5  ? L 8  ? 19 1 
1 F DC 2 1_555 H DG 3 1_555 -0.047 -0.001 0.105  -8.965  9.296   -0.074 15 K_DC6:DG7_L  K 6  ? L 7  ? 19 1 
1 F DG 3 1_555 H DC 2 1_555 0.031  0.014  0.061  9.214   9.897   0.133  16 K_DG7:DC6_L  K 7  ? L 6  ? 19 1 
1 F DG 4 1_555 H DC 1 1_555 -0.230 -0.085 0.350  10.636  -14.676 1.607  17 K_DG8:DC5_L  K 8  ? L 5  ? 19 1 
1 F DC 5 1_555 G DG 4 1_555 0.176  -0.151 -0.010 5.474   0.536   -1.566 18 K_DC9:DG4_H  K 9  ? H 4  ? 19 1 
1 F DG 6 1_555 G DC 3 1_555 -0.213 -0.169 0.364  -2.388  -22.785 0.880  19 K_DG10:DC3_H K 10 ? H 3  ? 19 1 
1 F DC 7 1_555 G DG 2 1_555 0.218  0.058  0.505  -20.279 -13.104 -1.145 20 K_DC11:DG2_H K 11 ? H 2  ? 19 1 
# 
loop_
_ndb_struct_na_base_pair_step.model_number 
_ndb_struct_na_base_pair_step.i_label_asym_id_1 
_ndb_struct_na_base_pair_step.i_label_comp_id_1 
_ndb_struct_na_base_pair_step.i_label_seq_id_1 
_ndb_struct_na_base_pair_step.i_symmetry_1 
_ndb_struct_na_base_pair_step.j_label_asym_id_1 
_ndb_struct_na_base_pair_step.j_label_comp_id_1 
_ndb_struct_na_base_pair_step.j_label_seq_id_1 
_ndb_struct_na_base_pair_step.j_symmetry_1 
_ndb_struct_na_base_pair_step.i_label_asym_id_2 
_ndb_struct_na_base_pair_step.i_label_comp_id_2 
_ndb_struct_na_base_pair_step.i_label_seq_id_2 
_ndb_struct_na_base_pair_step.i_symmetry_2 
_ndb_struct_na_base_pair_step.j_label_asym_id_2 
_ndb_struct_na_base_pair_step.j_label_comp_id_2 
_ndb_struct_na_base_pair_step.j_label_seq_id_2 
_ndb_struct_na_base_pair_step.j_symmetry_2 
_ndb_struct_na_base_pair_step.shift 
_ndb_struct_na_base_pair_step.slide 
_ndb_struct_na_base_pair_step.rise 
_ndb_struct_na_base_pair_step.tilt 
_ndb_struct_na_base_pair_step.roll 
_ndb_struct_na_base_pair_step.twist 
_ndb_struct_na_base_pair_step.x_displacement 
_ndb_struct_na_base_pair_step.y_displacement 
_ndb_struct_na_base_pair_step.helical_rise 
_ndb_struct_na_base_pair_step.inclination 
_ndb_struct_na_base_pair_step.tip 
_ndb_struct_na_base_pair_step.helical_twist 
_ndb_struct_na_base_pair_step.step_number 
_ndb_struct_na_base_pair_step.step_name 
_ndb_struct_na_base_pair_step.i_auth_asym_id_1 
_ndb_struct_na_base_pair_step.i_auth_seq_id_1 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.j_auth_asym_id_1 
_ndb_struct_na_base_pair_step.j_auth_seq_id_1 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.i_auth_asym_id_2 
_ndb_struct_na_base_pair_step.i_auth_seq_id_2 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_2 
_ndb_struct_na_base_pair_step.j_auth_asym_id_2 
_ndb_struct_na_base_pair_step.j_auth_seq_id_2 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_2 
1 A DG 2 1_555 D DC 7 1_555 A DC 3 1_555 D DG 6 1_555 0.686  2.057  3.492 -2.343 2.170   36.256 2.967  -1.451 3.555 3.479   3.756  
36.392 1  EE_DG2DC3:DG10DC11_JJ E 2  ? J 11 ? E 3  ? J 10 ? 
1 A DC 3 1_555 D DG 6 1_555 A DG 4 1_555 D DC 5 1_555 0.409  2.829  3.476 2.147  -9.708  46.480 4.284  -0.338 2.878 -12.138 -2.684 
47.473 2  EE_DC3DG4:DC9DG10_JJ  E 3  ? J 10 ? E 4  ? J 9  ? 
1 A DG 4 1_555 D DC 5 1_555 B DC 1 1_555 D DG 4 1_555 -0.843 0.154  3.602 -6.064 3.954   38.088 -0.312 0.436  3.686 5.992   9.190  
38.745 3  EI_DG4DC5:DG8DC9_JJ   E 4  ? J 9  ? I 5  ? J 8  ? 
1 B DC 1 1_555 D DG 4 1_555 B DC 2 1_555 D DG 3 1_555 0.158  -0.381 3.596 2.399  7.187   29.273 -2.318 0.226  3.410 13.929  -4.650 
30.217 4  II_DC5DC6:DG7DG8_JJ   I 5  ? J 8  ? I 6  ? J 7  ? 
1 B DC 2 1_555 D DG 3 1_555 B DG 3 1_555 D DC 2 1_555 0.000  0.150  3.613 0.730  -20.707 39.193 2.345  0.076  3.157 -28.576 -1.007 
44.142 5  II_DC6DG7:DC6DG7_JJ   I 6  ? J 7  ? I 7  ? J 6  ? 
1 B DG 3 1_555 D DC 2 1_555 B DG 4 1_555 D DC 1 1_555 -0.097 -0.293 3.595 -2.352 6.988   28.309 -2.233 -0.364 3.423 13.990  4.708  
29.235 6  II_DG7DG8:DC5DC6_JJ   I 7  ? J 6  ? I 8  ? J 5  ? 
1 B DG 4 1_555 D DC 1 1_555 B DC 5 1_555 C DG 4 1_555 0.785  0.003  3.599 5.333  3.498   37.832 -0.484 -0.450 3.658 5.349   -8.154 
38.346 7  II_DG8DC9:DG4DC5_FJ   I 8  ? J 5  ? I 9  ? F 4  ? 
1 B DC 5 1_555 C DG 4 1_555 B DG 6 1_555 C DC 3 1_555 -0.246 2.977  3.421 -0.544 -7.316  46.961 4.273  0.263  2.954 -9.115  0.677  
47.498 8  II_DC9DG10:DC3DG4_FF  I 9  ? F 4  ? I 10 ? F 3  ? 
1 B DG 6 1_555 C DC 3 1_555 B DC 7 1_555 C DG 2 1_555 -0.382 0.911  3.321 -3.573 -2.476  34.959 1.878  0.094  3.273 -4.101  5.920  
35.220 9  II_DG10DC11:DG2DC3_FF I 10 ? F 3  ? I 11 ? F 2  ? 
1 E DG 2 1_555 H DC 7 1_555 E DC 3 1_555 H DG 6 1_555 -0.893 1.074  3.561 -1.258 -11.757 43.692 2.505  1.044  3.207 -15.463 1.655  
45.188 10 GG_DG2DC3:DG10DC11_LL G 2  ? L 11 ? G 3  ? L 10 ? 
1 E DC 3 1_555 H DG 6 1_555 E DG 4 1_555 H DC 5 1_555 1.481  1.203  3.448 5.569  -4.484  38.949 2.336  -1.491 3.465 -6.656  -8.267 
39.575 11 GG_DC3DG4:DC9DG10_LL  G 3  ? L 10 ? G 4  ? L 9  ? 
1 E DG 4 1_555 H DC 5 1_555 F DC 1 1_555 H DG 4 1_555 -0.726 -0.072 3.540 -5.385 2.849   36.514 -0.534 0.349  3.592 4.509   8.521  
37.002 12 GK_DG4DC5:DG8DC9_LL   G 4  ? L 9  ? K 5  ? L 8  ? 
1 F DC 1 1_555 H DG 4 1_555 F DC 2 1_555 H DG 3 1_555 0.183  -0.377 3.538 2.702  7.898   28.948 -2.455 0.239  3.325 15.400  -5.268 
30.103 13 KK_DC5DC6:DG7DG8_LL   K 5  ? L 8  ? K 6  ? L 7  ? 
1 F DC 2 1_555 H DG 3 1_555 F DG 3 1_555 H DC 2 1_555 -0.008 0.053  3.632 -0.042 -18.698 39.281 2.103  0.007  3.284 -26.096 0.058  
43.345 14 KK_DC6DG7:DC6DG7_LL   K 6  ? L 7  ? K 7  ? L 6  ? 
1 F DG 3 1_555 H DC 2 1_555 F DG 4 1_555 H DC 1 1_555 -0.315 -0.349 3.478 -3.296 8.214   29.313 -2.377 -0.092 3.277 15.784  6.334  
30.592 15 KK_DG7DG8:DC5DC6_LL   K 7  ? L 6  ? K 8  ? L 5  ? 
1 F DG 4 1_555 H DC 1 1_555 F DC 5 1_555 G DG 4 1_555 0.679  0.208  3.497 5.191  2.365   37.232 -0.011 -0.321 3.562 3.677   -8.072 
37.651 16 KK_DG8DC9:DG4DC5_HL   K 8  ? L 5  ? K 9  ? H 4  ? 
1 F DC 5 1_555 G DG 4 1_555 F DG 6 1_555 G DC 3 1_555 -0.507 3.066  3.634 -0.968 -7.354  46.248 4.496  0.555  3.148 -9.292  1.223  
46.807 17 KK_DC9DG10:DC3DG4_HH  K 9  ? H 4  ? K 10 ? H 3  ? 
1 F DG 6 1_555 G DC 3 1_555 F DC 7 1_555 G DG 2 1_555 -0.343 0.672  3.695 -4.104 -7.725  43.504 1.694  0.028  3.548 -10.299 5.470  
44.333 18 KK_DG10DC11:DG2DC3_HH K 10 ? H 3  ? K 11 ? H 2  ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'MAGNESIUM ION' MG  
5 'ACETIC ACID'   ACY 
6 water           HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
M  4 MG  1   2222 2222 MG  MG  I . 
N  4 MG  1   4444 4444 MG  MG  J . 
O  4 MG  1   6666 6666 MG  MG  K . 
P  4 MG  1   8888 8888 MG  MG  L . 
Q  4 MG  1   5555 5555 MG  MG  A . 
R  5 ACY 1   2001 2001 ACY ACY A . 
S  4 MG  1   3333 3333 MG  MG  B . 
T  5 ACY 1   3002 3002 ACY ACY B . 
U  4 MG  1   7777 7777 MG  MG  C . 
V  5 ACY 1   4003 4003 ACY ACY C . 
W  4 MG  1   9999 9999 MG  MG  D . 
X  5 ACY 1   5004 5004 ACY ACY D . 
Y  6 HOH 1   58   58   HOH HOH E . 
Y  6 HOH 2   261  261  HOH HOH E . 
Y  6 HOH 3   284  284  HOH HOH E . 
Y  6 HOH 4   385  385  HOH HOH E . 
Y  6 HOH 5   434  434  HOH HOH E . 
Y  6 HOH 6   436  436  HOH HOH E . 
Y  6 HOH 7   438  438  HOH HOH E . 
Y  6 HOH 8   439  439  HOH HOH E . 
Y  6 HOH 9   440  440  HOH HOH E . 
Y  6 HOH 10  453  453  HOH HOH E . 
Y  6 HOH 11  455  455  HOH HOH E . 
Y  6 HOH 12  570  570  HOH HOH E . 
Y  6 HOH 13  625  625  HOH HOH E . 
Y  6 HOH 14  630  630  HOH HOH E . 
Y  6 HOH 15  1100 1100 HOH HOH E . 
Z  6 HOH 1   18   18   HOH HOH I . 
Z  6 HOH 2   42   42   HOH HOH I . 
Z  6 HOH 3   54   54   HOH HOH I . 
Z  6 HOH 4   56   56   HOH HOH I . 
Z  6 HOH 5   57   57   HOH HOH I . 
Z  6 HOH 6   143  143  HOH HOH I . 
Z  6 HOH 7   145  145  HOH HOH I . 
Z  6 HOH 8   200  200  HOH HOH I . 
Z  6 HOH 9   222  222  HOH HOH I . 
Z  6 HOH 10  230  230  HOH HOH I . 
Z  6 HOH 11  259  259  HOH HOH I . 
Z  6 HOH 12  266  266  HOH HOH I . 
Z  6 HOH 13  298  298  HOH HOH I . 
Z  6 HOH 14  360  360  HOH HOH I . 
Z  6 HOH 15  390  390  HOH HOH I . 
Z  6 HOH 16  404  404  HOH HOH I . 
Z  6 HOH 17  411  411  HOH HOH I . 
Z  6 HOH 18  414  414  HOH HOH I . 
Z  6 HOH 19  419  419  HOH HOH I . 
Z  6 HOH 20  443  443  HOH HOH I . 
Z  6 HOH 21  444  444  HOH HOH I . 
Z  6 HOH 22  445  445  HOH HOH I . 
Z  6 HOH 23  446  446  HOH HOH I . 
Z  6 HOH 24  675  675  HOH HOH I . 
Z  6 HOH 25  676  676  HOH HOH I . 
Z  6 HOH 26  677  677  HOH HOH I . 
Z  6 HOH 27  933  933  HOH HOH I . 
Z  6 HOH 28  934  934  HOH HOH I . 
Z  6 HOH 29  935  935  HOH HOH I . 
Z  6 HOH 30  937  937  HOH HOH I . 
Z  6 HOH 31  938  938  HOH HOH I . 
Z  6 HOH 32  939  939  HOH HOH I . 
Z  6 HOH 33  1002 1002 HOH HOH I . 
Z  6 HOH 34  1105 1105 HOH HOH I . 
Z  6 HOH 35  1242 1242 HOH HOH I . 
Z  6 HOH 36  1279 1279 HOH HOH I . 
AA 6 HOH 1   22   22   HOH HOH F . 
AA 6 HOH 2   45   45   HOH HOH F . 
AA 6 HOH 3   116  116  HOH HOH F . 
AA 6 HOH 4   406  406  HOH HOH F . 
AA 6 HOH 5   765  765  HOH HOH F . 
AA 6 HOH 6   766  766  HOH HOH F . 
AA 6 HOH 7   767  767  HOH HOH F . 
AA 6 HOH 8   1064 1064 HOH HOH F . 
AA 6 HOH 9   1080 1080 HOH HOH F . 
AA 6 HOH 10  1097 1097 HOH HOH F . 
AA 6 HOH 11  1277 1277 HOH HOH F . 
AA 6 HOH 12  1278 1278 HOH HOH F . 
BA 6 HOH 1   43   43   HOH HOH J . 
BA 6 HOH 2   221  221  HOH HOH J . 
BA 6 HOH 3   236  236  HOH HOH J . 
BA 6 HOH 4   253  253  HOH HOH J . 
BA 6 HOH 5   268  268  HOH HOH J . 
BA 6 HOH 6   282  282  HOH HOH J . 
BA 6 HOH 7   332  332  HOH HOH J . 
BA 6 HOH 8   389  389  HOH HOH J . 
BA 6 HOH 9   393  393  HOH HOH J . 
BA 6 HOH 10  396  396  HOH HOH J . 
BA 6 HOH 11  400  400  HOH HOH J . 
BA 6 HOH 12  407  407  HOH HOH J . 
BA 6 HOH 13  412  412  HOH HOH J . 
BA 6 HOH 14  415  415  HOH HOH J . 
BA 6 HOH 15  416  416  HOH HOH J . 
BA 6 HOH 16  417  417  HOH HOH J . 
BA 6 HOH 17  418  418  HOH HOH J . 
BA 6 HOH 18  421  421  HOH HOH J . 
BA 6 HOH 19  422  422  HOH HOH J . 
BA 6 HOH 20  425  425  HOH HOH J . 
BA 6 HOH 21  427  427  HOH HOH J . 
BA 6 HOH 22  429  429  HOH HOH J . 
BA 6 HOH 23  430  430  HOH HOH J . 
BA 6 HOH 24  431  431  HOH HOH J . 
BA 6 HOH 25  433  433  HOH HOH J . 
BA 6 HOH 26  435  435  HOH HOH J . 
BA 6 HOH 27  450  450  HOH HOH J . 
BA 6 HOH 28  457  457  HOH HOH J . 
BA 6 HOH 29  632  632  HOH HOH J . 
BA 6 HOH 30  942  942  HOH HOH J . 
BA 6 HOH 31  943  943  HOH HOH J . 
BA 6 HOH 32  944  944  HOH HOH J . 
BA 6 HOH 33  945  945  HOH HOH J . 
BA 6 HOH 34  946  946  HOH HOH J . 
BA 6 HOH 35  1216 1216 HOH HOH J . 
CA 6 HOH 1   5    1    HOH HOH G . 
CA 6 HOH 2   6    25   HOH HOH G . 
CA 6 HOH 3   7    59   HOH HOH G . 
CA 6 HOH 4   8    119  HOH HOH G . 
CA 6 HOH 5   9    147  HOH HOH G . 
CA 6 HOH 6   10   153  HOH HOH G . 
CA 6 HOH 7   11   179  HOH HOH G . 
CA 6 HOH 8   12   189  HOH HOH G . 
CA 6 HOH 9   13   213  HOH HOH G . 
CA 6 HOH 10  14   227  HOH HOH G . 
CA 6 HOH 11  15   303  HOH HOH G . 
CA 6 HOH 12  16   955  HOH HOH G . 
CA 6 HOH 13  17   957  HOH HOH G . 
CA 6 HOH 14  18   1215 HOH HOH G . 
DA 6 HOH 1   67   67   HOH HOH K . 
DA 6 HOH 2   238  238  HOH HOH K . 
DA 6 HOH 3   271  271  HOH HOH K . 
DA 6 HOH 4   281  281  HOH HOH K . 
DA 6 HOH 5   295  295  HOH HOH K . 
DA 6 HOH 6   300  300  HOH HOH K . 
DA 6 HOH 7   304  304  HOH HOH K . 
DA 6 HOH 8   313  313  HOH HOH K . 
DA 6 HOH 9   328  328  HOH HOH K . 
DA 6 HOH 10  329  329  HOH HOH K . 
DA 6 HOH 11  346  346  HOH HOH K . 
DA 6 HOH 12  365  365  HOH HOH K . 
DA 6 HOH 13  378  378  HOH HOH K . 
DA 6 HOH 14  459  459  HOH HOH K . 
DA 6 HOH 15  461  461  HOH HOH K . 
DA 6 HOH 16  462  462  HOH HOH K . 
DA 6 HOH 17  463  463  HOH HOH K . 
DA 6 HOH 18  465  465  HOH HOH K . 
DA 6 HOH 19  472  472  HOH HOH K . 
DA 6 HOH 20  473  473  HOH HOH K . 
DA 6 HOH 21  475  475  HOH HOH K . 
DA 6 HOH 22  482  482  HOH HOH K . 
DA 6 HOH 23  485  485  HOH HOH K . 
DA 6 HOH 24  562  562  HOH HOH K . 
DA 6 HOH 25  563  563  HOH HOH K . 
DA 6 HOH 26  813  813  HOH HOH K . 
DA 6 HOH 27  814  814  HOH HOH K . 
DA 6 HOH 28  815  815  HOH HOH K . 
DA 6 HOH 29  816  816  HOH HOH K . 
DA 6 HOH 30  828  828  HOH HOH K . 
DA 6 HOH 31  1098 1098 HOH HOH K . 
DA 6 HOH 32  1192 1192 HOH HOH K . 
EA 6 HOH 1   73   73   HOH HOH H . 
EA 6 HOH 2   203  203  HOH HOH H . 
EA 6 HOH 3   255  255  HOH HOH H . 
EA 6 HOH 4   349  349  HOH HOH H . 
EA 6 HOH 5   812  812  HOH HOH H . 
EA 6 HOH 6   817  817  HOH HOH H . 
EA 6 HOH 7   818  818  HOH HOH H . 
EA 6 HOH 8   819  819  HOH HOH H . 
EA 6 HOH 9   824  824  HOH HOH H . 
EA 6 HOH 10  825  825  HOH HOH H . 
EA 6 HOH 11  899  899  HOH HOH H . 
EA 6 HOH 12  947  947  HOH HOH H . 
EA 6 HOH 13  1068 1068 HOH HOH H . 
EA 6 HOH 14  1223 1223 HOH HOH H . 
EA 6 HOH 15  1250 1250 HOH HOH H . 
EA 6 HOH 16  1251 1251 HOH HOH H . 
EA 6 HOH 17  1252 1252 HOH HOH H . 
FA 6 HOH 1   32   32   HOH HOH L . 
FA 6 HOH 2   52   52   HOH HOH L . 
FA 6 HOH 3   55   55   HOH HOH L . 
FA 6 HOH 4   170  170  HOH HOH L . 
FA 6 HOH 5   177  177  HOH HOH L . 
FA 6 HOH 6   178  178  HOH HOH L . 
FA 6 HOH 7   202  202  HOH HOH L . 
FA 6 HOH 8   251  251  HOH HOH L . 
FA 6 HOH 9   270  270  HOH HOH L . 
FA 6 HOH 10  275  275  HOH HOH L . 
FA 6 HOH 11  280  280  HOH HOH L . 
FA 6 HOH 12  302  302  HOH HOH L . 
FA 6 HOH 13  317  317  HOH HOH L . 
FA 6 HOH 14  347  347  HOH HOH L . 
FA 6 HOH 15  387  387  HOH HOH L . 
FA 6 HOH 16  458  458  HOH HOH L . 
FA 6 HOH 17  460  460  HOH HOH L . 
FA 6 HOH 18  464  464  HOH HOH L . 
FA 6 HOH 19  466  466  HOH HOH L . 
FA 6 HOH 20  467  467  HOH HOH L . 
FA 6 HOH 21  469  469  HOH HOH L . 
FA 6 HOH 22  470  470  HOH HOH L . 
FA 6 HOH 23  888  888  HOH HOH L . 
FA 6 HOH 24  896  896  HOH HOH L . 
FA 6 HOH 25  949  949  HOH HOH L . 
FA 6 HOH 26  950  950  HOH HOH L . 
FA 6 HOH 27  951  951  HOH HOH L . 
FA 6 HOH 28  952  952  HOH HOH L . 
FA 6 HOH 29  1026 1026 HOH HOH L . 
FA 6 HOH 30  1073 1073 HOH HOH L . 
FA 6 HOH 31  1217 1217 HOH HOH L . 
FA 6 HOH 32  1233 1233 HOH HOH L . 
GA 6 HOH 1   5556 7    HOH HOH A . 
GA 6 HOH 2   5557 12   HOH HOH A . 
GA 6 HOH 3   5558 13   HOH HOH A . 
GA 6 HOH 4   5559 20   HOH HOH A . 
GA 6 HOH 5   5560 21   HOH HOH A . 
GA 6 HOH 6   5561 27   HOH HOH A . 
GA 6 HOH 7   5562 30   HOH HOH A . 
GA 6 HOH 8   5563 34   HOH HOH A . 
GA 6 HOH 9   5564 38   HOH HOH A . 
GA 6 HOH 10  5565 50   HOH HOH A . 
GA 6 HOH 11  5566 65   HOH HOH A . 
GA 6 HOH 12  5567 71   HOH HOH A . 
GA 6 HOH 13  5568 74   HOH HOH A . 
GA 6 HOH 14  5569 75   HOH HOH A . 
GA 6 HOH 15  5570 77   HOH HOH A . 
GA 6 HOH 16  5571 78   HOH HOH A . 
GA 6 HOH 17  5572 87   HOH HOH A . 
GA 6 HOH 18  5573 99   HOH HOH A . 
GA 6 HOH 19  5574 103  HOH HOH A . 
GA 6 HOH 20  5575 107  HOH HOH A . 
GA 6 HOH 21  5576 109  HOH HOH A . 
GA 6 HOH 22  5577 110  HOH HOH A . 
GA 6 HOH 23  5578 123  HOH HOH A . 
GA 6 HOH 24  5579 128  HOH HOH A . 
GA 6 HOH 25  5580 133  HOH HOH A . 
GA 6 HOH 26  5581 134  HOH HOH A . 
GA 6 HOH 27  5582 135  HOH HOH A . 
GA 6 HOH 28  5583 136  HOH HOH A . 
GA 6 HOH 29  5584 144  HOH HOH A . 
GA 6 HOH 30  5585 146  HOH HOH A . 
GA 6 HOH 31  5586 156  HOH HOH A . 
GA 6 HOH 32  5587 160  HOH HOH A . 
GA 6 HOH 33  5588 164  HOH HOH A . 
GA 6 HOH 34  5589 167  HOH HOH A . 
GA 6 HOH 35  5590 173  HOH HOH A . 
GA 6 HOH 36  5591 187  HOH HOH A . 
GA 6 HOH 37  5592 196  HOH HOH A . 
GA 6 HOH 38  5593 199  HOH HOH A . 
GA 6 HOH 39  5594 205  HOH HOH A . 
GA 6 HOH 40  5595 206  HOH HOH A . 
GA 6 HOH 41  5596 212  HOH HOH A . 
GA 6 HOH 42  5597 223  HOH HOH A . 
GA 6 HOH 43  5598 224  HOH HOH A . 
GA 6 HOH 44  5599 234  HOH HOH A . 
GA 6 HOH 45  5600 237  HOH HOH A . 
GA 6 HOH 46  5601 243  HOH HOH A . 
GA 6 HOH 47  5602 262  HOH HOH A . 
GA 6 HOH 48  5603 263  HOH HOH A . 
GA 6 HOH 49  5604 289  HOH HOH A . 
GA 6 HOH 50  5605 290  HOH HOH A . 
GA 6 HOH 51  5606 299  HOH HOH A . 
GA 6 HOH 52  5607 306  HOH HOH A . 
GA 6 HOH 53  5608 312  HOH HOH A . 
GA 6 HOH 54  5609 323  HOH HOH A . 
GA 6 HOH 55  5610 324  HOH HOH A . 
GA 6 HOH 56  5611 325  HOH HOH A . 
GA 6 HOH 57  5612 351  HOH HOH A . 
GA 6 HOH 58  5613 354  HOH HOH A . 
GA 6 HOH 59  5614 361  HOH HOH A . 
GA 6 HOH 60  5615 369  HOH HOH A . 
GA 6 HOH 61  5616 373  HOH HOH A . 
GA 6 HOH 62  5617 374  HOH HOH A . 
GA 6 HOH 63  5618 375  HOH HOH A . 
GA 6 HOH 64  5619 376  HOH HOH A . 
GA 6 HOH 65  5620 383  HOH HOH A . 
GA 6 HOH 66  5621 391  HOH HOH A . 
GA 6 HOH 67  5622 392  HOH HOH A . 
GA 6 HOH 68  5623 394  HOH HOH A . 
GA 6 HOH 69  5624 395  HOH HOH A . 
GA 6 HOH 70  5625 397  HOH HOH A . 
GA 6 HOH 71  5626 398  HOH HOH A . 
GA 6 HOH 72  5627 399  HOH HOH A . 
GA 6 HOH 73  5628 401  HOH HOH A . 
GA 6 HOH 74  5629 402  HOH HOH A . 
GA 6 HOH 75  5630 403  HOH HOH A . 
GA 6 HOH 76  5631 405  HOH HOH A . 
GA 6 HOH 77  5632 408  HOH HOH A . 
GA 6 HOH 78  5633 409  HOH HOH A . 
GA 6 HOH 79  5634 410  HOH HOH A . 
GA 6 HOH 80  5635 413  HOH HOH A . 
GA 6 HOH 81  5636 426  HOH HOH A . 
GA 6 HOH 82  5637 428  HOH HOH A . 
GA 6 HOH 83  5638 432  HOH HOH A . 
GA 6 HOH 84  5639 437  HOH HOH A . 
GA 6 HOH 85  5640 448  HOH HOH A . 
GA 6 HOH 86  5641 449  HOH HOH A . 
GA 6 HOH 87  5642 451  HOH HOH A . 
GA 6 HOH 88  5643 454  HOH HOH A . 
GA 6 HOH 89  5644 503  HOH HOH A . 
GA 6 HOH 90  5645 504  HOH HOH A . 
GA 6 HOH 91  5646 505  HOH HOH A . 
GA 6 HOH 92  5647 508  HOH HOH A . 
GA 6 HOH 93  5648 523  HOH HOH A . 
GA 6 HOH 94  5649 528  HOH HOH A . 
GA 6 HOH 95  5650 529  HOH HOH A . 
GA 6 HOH 96  5651 530  HOH HOH A . 
GA 6 HOH 97  5652 538  HOH HOH A . 
GA 6 HOH 98  5653 539  HOH HOH A . 
GA 6 HOH 99  5654 540  HOH HOH A . 
GA 6 HOH 100 5655 541  HOH HOH A . 
GA 6 HOH 101 5656 542  HOH HOH A . 
GA 6 HOH 102 5657 544  HOH HOH A . 
GA 6 HOH 103 5658 545  HOH HOH A . 
GA 6 HOH 104 5659 546  HOH HOH A . 
GA 6 HOH 105 5660 548  HOH HOH A . 
GA 6 HOH 106 5661 558  HOH HOH A . 
GA 6 HOH 107 5662 565  HOH HOH A . 
GA 6 HOH 108 5663 566  HOH HOH A . 
GA 6 HOH 109 5664 567  HOH HOH A . 
GA 6 HOH 110 5665 568  HOH HOH A . 
GA 6 HOH 111 5666 569  HOH HOH A . 
GA 6 HOH 112 5667 571  HOH HOH A . 
GA 6 HOH 113 5668 572  HOH HOH A . 
GA 6 HOH 114 5669 573  HOH HOH A . 
GA 6 HOH 115 5670 574  HOH HOH A . 
GA 6 HOH 116 5671 575  HOH HOH A . 
GA 6 HOH 117 5672 576  HOH HOH A . 
GA 6 HOH 118 5673 577  HOH HOH A . 
GA 6 HOH 119 5674 578  HOH HOH A . 
GA 6 HOH 120 5675 579  HOH HOH A . 
GA 6 HOH 121 5676 580  HOH HOH A . 
GA 6 HOH 122 5677 581  HOH HOH A . 
GA 6 HOH 123 5678 582  HOH HOH A . 
GA 6 HOH 124 5679 583  HOH HOH A . 
GA 6 HOH 125 5680 584  HOH HOH A . 
GA 6 HOH 126 5681 585  HOH HOH A . 
GA 6 HOH 127 5682 586  HOH HOH A . 
GA 6 HOH 128 5683 588  HOH HOH A . 
GA 6 HOH 129 5684 589  HOH HOH A . 
GA 6 HOH 130 5685 590  HOH HOH A . 
GA 6 HOH 131 5686 591  HOH HOH A . 
GA 6 HOH 132 5687 592  HOH HOH A . 
GA 6 HOH 133 5688 594  HOH HOH A . 
GA 6 HOH 134 5689 596  HOH HOH A . 
GA 6 HOH 135 5690 597  HOH HOH A . 
GA 6 HOH 136 5691 598  HOH HOH A . 
GA 6 HOH 137 5692 599  HOH HOH A . 
GA 6 HOH 138 5693 600  HOH HOH A . 
GA 6 HOH 139 5694 601  HOH HOH A . 
GA 6 HOH 140 5695 602  HOH HOH A . 
GA 6 HOH 141 5696 603  HOH HOH A . 
GA 6 HOH 142 5697 604  HOH HOH A . 
GA 6 HOH 143 5698 605  HOH HOH A . 
GA 6 HOH 144 5699 606  HOH HOH A . 
GA 6 HOH 145 5700 607  HOH HOH A . 
GA 6 HOH 146 5701 608  HOH HOH A . 
GA 6 HOH 147 5702 609  HOH HOH A . 
GA 6 HOH 148 5703 610  HOH HOH A . 
GA 6 HOH 149 5704 611  HOH HOH A . 
GA 6 HOH 150 5705 612  HOH HOH A . 
GA 6 HOH 151 5706 613  HOH HOH A . 
GA 6 HOH 152 5707 614  HOH HOH A . 
GA 6 HOH 153 5708 617  HOH HOH A . 
GA 6 HOH 154 5709 618  HOH HOH A . 
GA 6 HOH 155 5710 620  HOH HOH A . 
GA 6 HOH 156 5711 621  HOH HOH A . 
GA 6 HOH 157 5712 628  HOH HOH A . 
GA 6 HOH 158 5713 629  HOH HOH A . 
GA 6 HOH 159 5714 634  HOH HOH A . 
GA 6 HOH 160 5715 638  HOH HOH A . 
GA 6 HOH 161 5716 639  HOH HOH A . 
GA 6 HOH 162 5717 642  HOH HOH A . 
GA 6 HOH 163 5718 643  HOH HOH A . 
GA 6 HOH 164 5719 645  HOH HOH A . 
GA 6 HOH 165 5720 646  HOH HOH A . 
GA 6 HOH 166 5721 647  HOH HOH A . 
GA 6 HOH 167 5722 648  HOH HOH A . 
GA 6 HOH 168 5723 649  HOH HOH A . 
GA 6 HOH 169 5724 650  HOH HOH A . 
GA 6 HOH 170 5725 651  HOH HOH A . 
GA 6 HOH 171 5726 652  HOH HOH A . 
GA 6 HOH 172 5727 653  HOH HOH A . 
GA 6 HOH 173 5728 654  HOH HOH A . 
GA 6 HOH 174 5729 655  HOH HOH A . 
GA 6 HOH 175 5730 656  HOH HOH A . 
GA 6 HOH 176 5731 768  HOH HOH A . 
GA 6 HOH 177 5732 777  HOH HOH A . 
GA 6 HOH 178 5733 791  HOH HOH A . 
GA 6 HOH 179 5734 879  HOH HOH A . 
GA 6 HOH 180 5735 880  HOH HOH A . 
GA 6 HOH 181 5736 917  HOH HOH A . 
GA 6 HOH 182 5737 918  HOH HOH A . 
GA 6 HOH 183 5738 931  HOH HOH A . 
GA 6 HOH 184 5739 932  HOH HOH A . 
GA 6 HOH 185 5740 936  HOH HOH A . 
GA 6 HOH 186 5741 940  HOH HOH A . 
GA 6 HOH 187 5742 941  HOH HOH A . 
GA 6 HOH 188 5743 959  HOH HOH A . 
GA 6 HOH 189 5744 960  HOH HOH A . 
GA 6 HOH 190 5745 961  HOH HOH A . 
GA 6 HOH 191 5746 962  HOH HOH A . 
GA 6 HOH 192 5747 963  HOH HOH A . 
GA 6 HOH 193 5748 964  HOH HOH A . 
GA 6 HOH 194 5749 965  HOH HOH A . 
GA 6 HOH 195 5750 966  HOH HOH A . 
GA 6 HOH 196 5751 967  HOH HOH A . 
GA 6 HOH 197 5752 969  HOH HOH A . 
GA 6 HOH 198 5753 970  HOH HOH A . 
GA 6 HOH 199 5754 971  HOH HOH A . 
GA 6 HOH 200 5755 972  HOH HOH A . 
GA 6 HOH 201 5756 973  HOH HOH A . 
GA 6 HOH 202 5757 974  HOH HOH A . 
GA 6 HOH 203 5758 975  HOH HOH A . 
GA 6 HOH 204 5759 976  HOH HOH A . 
GA 6 HOH 205 5760 977  HOH HOH A . 
GA 6 HOH 206 5761 978  HOH HOH A . 
GA 6 HOH 207 5762 979  HOH HOH A . 
GA 6 HOH 208 5763 982  HOH HOH A . 
GA 6 HOH 209 5764 983  HOH HOH A . 
GA 6 HOH 210 5765 985  HOH HOH A . 
GA 6 HOH 211 5766 987  HOH HOH A . 
GA 6 HOH 212 5767 988  HOH HOH A . 
GA 6 HOH 213 5768 989  HOH HOH A . 
GA 6 HOH 214 5769 990  HOH HOH A . 
GA 6 HOH 215 5770 991  HOH HOH A . 
GA 6 HOH 216 5771 992  HOH HOH A . 
GA 6 HOH 217 5772 994  HOH HOH A . 
GA 6 HOH 218 5773 997  HOH HOH A . 
GA 6 HOH 219 5774 1014 HOH HOH A . 
GA 6 HOH 220 5775 1017 HOH HOH A . 
GA 6 HOH 221 5776 1043 HOH HOH A . 
GA 6 HOH 222 5777 1050 HOH HOH A . 
GA 6 HOH 223 5778 1065 HOH HOH A . 
GA 6 HOH 224 5779 1066 HOH HOH A . 
GA 6 HOH 225 5780 1070 HOH HOH A . 
GA 6 HOH 226 5781 1071 HOH HOH A . 
GA 6 HOH 227 5782 1079 HOH HOH A . 
GA 6 HOH 228 5783 1095 HOH HOH A . 
GA 6 HOH 229 5784 1101 HOH HOH A . 
GA 6 HOH 230 5785 1102 HOH HOH A . 
GA 6 HOH 231 5786 1103 HOH HOH A . 
GA 6 HOH 232 5787 1104 HOH HOH A . 
GA 6 HOH 233 5788 1106 HOH HOH A . 
GA 6 HOH 234 5789 1107 HOH HOH A . 
GA 6 HOH 235 5790 1108 HOH HOH A . 
GA 6 HOH 236 5791 1109 HOH HOH A . 
GA 6 HOH 237 5792 1110 HOH HOH A . 
GA 6 HOH 238 5793 1111 HOH HOH A . 
GA 6 HOH 239 5794 1112 HOH HOH A . 
GA 6 HOH 240 5795 1114 HOH HOH A . 
GA 6 HOH 241 5796 1115 HOH HOH A . 
GA 6 HOH 242 5797 1116 HOH HOH A . 
GA 6 HOH 243 5798 1117 HOH HOH A . 
GA 6 HOH 244 5799 1118 HOH HOH A . 
GA 6 HOH 245 5800 1119 HOH HOH A . 
GA 6 HOH 246 5801 1120 HOH HOH A . 
GA 6 HOH 247 5802 1121 HOH HOH A . 
GA 6 HOH 248 5803 1123 HOH HOH A . 
GA 6 HOH 249 5804 1125 HOH HOH A . 
GA 6 HOH 250 5805 1126 HOH HOH A . 
GA 6 HOH 251 5806 1195 HOH HOH A . 
GA 6 HOH 252 5807 1196 HOH HOH A . 
GA 6 HOH 253 5808 1237 HOH HOH A . 
GA 6 HOH 254 5809 1238 HOH HOH A . 
GA 6 HOH 255 5810 1239 HOH HOH A . 
GA 6 HOH 256 5811 1240 HOH HOH A . 
GA 6 HOH 257 5812 1241 HOH HOH A . 
GA 6 HOH 258 5813 1244 HOH HOH A . 
HA 6 HOH 1   3334 8    HOH HOH B . 
HA 6 HOH 2   3335 10   HOH HOH B . 
HA 6 HOH 3   3336 19   HOH HOH B . 
HA 6 HOH 4   3337 24   HOH HOH B . 
HA 6 HOH 5   3338 29   HOH HOH B . 
HA 6 HOH 6   3339 35   HOH HOH B . 
HA 6 HOH 7   3340 36   HOH HOH B . 
HA 6 HOH 8   3341 48   HOH HOH B . 
HA 6 HOH 9   3342 62   HOH HOH B . 
HA 6 HOH 10  3343 68   HOH HOH B . 
HA 6 HOH 11  3344 70   HOH HOH B . 
HA 6 HOH 12  3345 84   HOH HOH B . 
HA 6 HOH 13  3346 89   HOH HOH B . 
HA 6 HOH 14  3347 102  HOH HOH B . 
HA 6 HOH 15  3348 111  HOH HOH B . 
HA 6 HOH 16  3349 124  HOH HOH B . 
HA 6 HOH 17  3350 127  HOH HOH B . 
HA 6 HOH 18  3351 129  HOH HOH B . 
HA 6 HOH 19  3352 130  HOH HOH B . 
HA 6 HOH 20  3353 132  HOH HOH B . 
HA 6 HOH 21  3354 137  HOH HOH B . 
HA 6 HOH 22  3355 138  HOH HOH B . 
HA 6 HOH 23  3356 141  HOH HOH B . 
HA 6 HOH 24  3357 151  HOH HOH B . 
HA 6 HOH 25  3358 158  HOH HOH B . 
HA 6 HOH 26  3359 159  HOH HOH B . 
HA 6 HOH 27  3360 166  HOH HOH B . 
HA 6 HOH 28  3361 175  HOH HOH B . 
HA 6 HOH 29  3362 176  HOH HOH B . 
HA 6 HOH 30  3363 184  HOH HOH B . 
HA 6 HOH 31  3364 185  HOH HOH B . 
HA 6 HOH 32  3365 186  HOH HOH B . 
HA 6 HOH 33  3366 197  HOH HOH B . 
HA 6 HOH 34  3367 198  HOH HOH B . 
HA 6 HOH 35  3368 208  HOH HOH B . 
HA 6 HOH 36  3369 209  HOH HOH B . 
HA 6 HOH 37  3370 216  HOH HOH B . 
HA 6 HOH 38  3371 229  HOH HOH B . 
HA 6 HOH 39  3372 231  HOH HOH B . 
HA 6 HOH 40  3373 233  HOH HOH B . 
HA 6 HOH 41  3374 235  HOH HOH B . 
HA 6 HOH 42  3375 248  HOH HOH B . 
HA 6 HOH 43  3376 260  HOH HOH B . 
HA 6 HOH 44  3377 267  HOH HOH B . 
HA 6 HOH 45  3378 272  HOH HOH B . 
HA 6 HOH 46  3379 274  HOH HOH B . 
HA 6 HOH 47  3380 278  HOH HOH B . 
HA 6 HOH 48  3381 287  HOH HOH B . 
HA 6 HOH 49  3382 293  HOH HOH B . 
HA 6 HOH 50  3383 294  HOH HOH B . 
HA 6 HOH 51  3384 305  HOH HOH B . 
HA 6 HOH 52  3385 310  HOH HOH B . 
HA 6 HOH 53  3386 315  HOH HOH B . 
HA 6 HOH 54  3387 316  HOH HOH B . 
HA 6 HOH 55  3388 320  HOH HOH B . 
HA 6 HOH 56  3389 322  HOH HOH B . 
HA 6 HOH 57  3390 330  HOH HOH B . 
HA 6 HOH 58  3391 333  HOH HOH B . 
HA 6 HOH 59  3392 334  HOH HOH B . 
HA 6 HOH 60  3393 335  HOH HOH B . 
HA 6 HOH 61  3394 336  HOH HOH B . 
HA 6 HOH 62  3395 343  HOH HOH B . 
HA 6 HOH 63  3396 350  HOH HOH B . 
HA 6 HOH 64  3397 357  HOH HOH B . 
HA 6 HOH 65  3398 358  HOH HOH B . 
HA 6 HOH 66  3399 363  HOH HOH B . 
HA 6 HOH 67  3400 368  HOH HOH B . 
HA 6 HOH 68  3401 379  HOH HOH B . 
HA 6 HOH 69  3402 382  HOH HOH B . 
HA 6 HOH 70  3403 388  HOH HOH B . 
HA 6 HOH 71  3404 420  HOH HOH B . 
HA 6 HOH 72  3405 423  HOH HOH B . 
HA 6 HOH 73  3406 424  HOH HOH B . 
HA 6 HOH 74  3407 441  HOH HOH B . 
HA 6 HOH 75  3408 442  HOH HOH B . 
HA 6 HOH 76  3409 447  HOH HOH B . 
HA 6 HOH 77  3410 452  HOH HOH B . 
HA 6 HOH 78  3411 456  HOH HOH B . 
HA 6 HOH 79  3412 496  HOH HOH B . 
HA 6 HOH 80  3413 497  HOH HOH B . 
HA 6 HOH 81  3414 498  HOH HOH B . 
HA 6 HOH 82  3415 501  HOH HOH B . 
HA 6 HOH 83  3416 511  HOH HOH B . 
HA 6 HOH 84  3417 515  HOH HOH B . 
HA 6 HOH 85  3418 516  HOH HOH B . 
HA 6 HOH 86  3419 517  HOH HOH B . 
HA 6 HOH 87  3420 518  HOH HOH B . 
HA 6 HOH 88  3421 519  HOH HOH B . 
HA 6 HOH 89  3422 534  HOH HOH B . 
HA 6 HOH 90  3423 537  HOH HOH B . 
HA 6 HOH 91  3424 543  HOH HOH B . 
HA 6 HOH 92  3425 547  HOH HOH B . 
HA 6 HOH 93  3426 549  HOH HOH B . 
HA 6 HOH 94  3427 550  HOH HOH B . 
HA 6 HOH 95  3428 564  HOH HOH B . 
HA 6 HOH 96  3429 622  HOH HOH B . 
HA 6 HOH 97  3430 626  HOH HOH B . 
HA 6 HOH 98  3431 627  HOH HOH B . 
HA 6 HOH 99  3432 631  HOH HOH B . 
HA 6 HOH 100 3433 633  HOH HOH B . 
HA 6 HOH 101 3434 635  HOH HOH B . 
HA 6 HOH 102 3435 637  HOH HOH B . 
HA 6 HOH 103 3436 660  HOH HOH B . 
HA 6 HOH 104 3437 661  HOH HOH B . 
HA 6 HOH 105 3438 662  HOH HOH B . 
HA 6 HOH 106 3439 663  HOH HOH B . 
HA 6 HOH 107 3440 664  HOH HOH B . 
HA 6 HOH 108 3441 665  HOH HOH B . 
HA 6 HOH 109 3442 666  HOH HOH B . 
HA 6 HOH 110 3443 667  HOH HOH B . 
HA 6 HOH 111 3444 668  HOH HOH B . 
HA 6 HOH 112 3445 669  HOH HOH B . 
HA 6 HOH 113 3446 670  HOH HOH B . 
HA 6 HOH 114 3447 671  HOH HOH B . 
HA 6 HOH 115 3448 672  HOH HOH B . 
HA 6 HOH 116 3449 673  HOH HOH B . 
HA 6 HOH 117 3450 674  HOH HOH B . 
HA 6 HOH 118 3451 678  HOH HOH B . 
HA 6 HOH 119 3452 679  HOH HOH B . 
HA 6 HOH 120 3453 680  HOH HOH B . 
HA 6 HOH 121 3454 681  HOH HOH B . 
HA 6 HOH 122 3455 682  HOH HOH B . 
HA 6 HOH 123 3456 683  HOH HOH B . 
HA 6 HOH 124 3457 684  HOH HOH B . 
HA 6 HOH 125 3458 685  HOH HOH B . 
HA 6 HOH 126 3459 686  HOH HOH B . 
HA 6 HOH 127 3460 687  HOH HOH B . 
HA 6 HOH 128 3461 688  HOH HOH B . 
HA 6 HOH 129 3462 689  HOH HOH B . 
HA 6 HOH 130 3463 690  HOH HOH B . 
HA 6 HOH 131 3464 691  HOH HOH B . 
HA 6 HOH 132 3465 692  HOH HOH B . 
HA 6 HOH 133 3466 693  HOH HOH B . 
HA 6 HOH 134 3467 694  HOH HOH B . 
HA 6 HOH 135 3468 695  HOH HOH B . 
HA 6 HOH 136 3469 696  HOH HOH B . 
HA 6 HOH 137 3470 697  HOH HOH B . 
HA 6 HOH 138 3471 698  HOH HOH B . 
HA 6 HOH 139 3472 699  HOH HOH B . 
HA 6 HOH 140 3473 700  HOH HOH B . 
HA 6 HOH 141 3474 701  HOH HOH B . 
HA 6 HOH 142 3475 702  HOH HOH B . 
HA 6 HOH 143 3476 703  HOH HOH B . 
HA 6 HOH 144 3477 705  HOH HOH B . 
HA 6 HOH 145 3478 708  HOH HOH B . 
HA 6 HOH 146 3479 710  HOH HOH B . 
HA 6 HOH 147 3480 711  HOH HOH B . 
HA 6 HOH 148 3481 712  HOH HOH B . 
HA 6 HOH 149 3482 713  HOH HOH B . 
HA 6 HOH 150 3483 714  HOH HOH B . 
HA 6 HOH 151 3484 715  HOH HOH B . 
HA 6 HOH 152 3485 716  HOH HOH B . 
HA 6 HOH 153 3486 717  HOH HOH B . 
HA 6 HOH 154 3487 718  HOH HOH B . 
HA 6 HOH 155 3488 719  HOH HOH B . 
HA 6 HOH 156 3489 720  HOH HOH B . 
HA 6 HOH 157 3490 721  HOH HOH B . 
HA 6 HOH 158 3491 722  HOH HOH B . 
HA 6 HOH 159 3492 723  HOH HOH B . 
HA 6 HOH 160 3493 724  HOH HOH B . 
HA 6 HOH 161 3494 725  HOH HOH B . 
HA 6 HOH 162 3495 726  HOH HOH B . 
HA 6 HOH 163 3496 727  HOH HOH B . 
HA 6 HOH 164 3497 728  HOH HOH B . 
HA 6 HOH 165 3498 729  HOH HOH B . 
HA 6 HOH 166 3499 730  HOH HOH B . 
HA 6 HOH 167 3500 731  HOH HOH B . 
HA 6 HOH 168 3501 732  HOH HOH B . 
HA 6 HOH 169 3502 733  HOH HOH B . 
HA 6 HOH 170 3503 734  HOH HOH B . 
HA 6 HOH 171 3504 735  HOH HOH B . 
HA 6 HOH 172 3505 736  HOH HOH B . 
HA 6 HOH 173 3506 737  HOH HOH B . 
HA 6 HOH 174 3507 738  HOH HOH B . 
HA 6 HOH 175 3508 739  HOH HOH B . 
HA 6 HOH 176 3509 740  HOH HOH B . 
HA 6 HOH 177 3510 741  HOH HOH B . 
HA 6 HOH 178 3511 742  HOH HOH B . 
HA 6 HOH 179 3512 743  HOH HOH B . 
HA 6 HOH 180 3513 744  HOH HOH B . 
HA 6 HOH 181 3514 745  HOH HOH B . 
HA 6 HOH 182 3515 747  HOH HOH B . 
HA 6 HOH 183 3516 748  HOH HOH B . 
HA 6 HOH 184 3517 750  HOH HOH B . 
HA 6 HOH 185 3518 751  HOH HOH B . 
HA 6 HOH 186 3519 752  HOH HOH B . 
HA 6 HOH 187 3520 753  HOH HOH B . 
HA 6 HOH 188 3521 755  HOH HOH B . 
HA 6 HOH 189 3522 756  HOH HOH B . 
HA 6 HOH 190 3523 757  HOH HOH B . 
HA 6 HOH 191 3524 759  HOH HOH B . 
HA 6 HOH 192 3525 764  HOH HOH B . 
HA 6 HOH 193 3526 769  HOH HOH B . 
HA 6 HOH 194 3527 771  HOH HOH B . 
HA 6 HOH 195 3528 772  HOH HOH B . 
HA 6 HOH 196 3529 773  HOH HOH B . 
HA 6 HOH 197 3530 775  HOH HOH B . 
HA 6 HOH 198 3531 778  HOH HOH B . 
HA 6 HOH 199 3532 780  HOH HOH B . 
HA 6 HOH 200 3533 781  HOH HOH B . 
HA 6 HOH 201 3534 783  HOH HOH B . 
HA 6 HOH 202 3535 784  HOH HOH B . 
HA 6 HOH 203 3536 785  HOH HOH B . 
HA 6 HOH 204 3537 786  HOH HOH B . 
HA 6 HOH 205 3538 787  HOH HOH B . 
HA 6 HOH 206 3539 788  HOH HOH B . 
HA 6 HOH 207 3540 789  HOH HOH B . 
HA 6 HOH 208 3541 790  HOH HOH B . 
HA 6 HOH 209 3542 794  HOH HOH B . 
HA 6 HOH 210 3543 831  HOH HOH B . 
HA 6 HOH 211 3544 878  HOH HOH B . 
HA 6 HOH 212 3545 920  HOH HOH B . 
HA 6 HOH 213 3546 981  HOH HOH B . 
HA 6 HOH 214 3547 984  HOH HOH B . 
HA 6 HOH 215 3548 986  HOH HOH B . 
HA 6 HOH 216 3549 998  HOH HOH B . 
HA 6 HOH 217 3550 999  HOH HOH B . 
HA 6 HOH 218 3551 1000 HOH HOH B . 
HA 6 HOH 219 3552 1001 HOH HOH B . 
HA 6 HOH 220 3553 1003 HOH HOH B . 
HA 6 HOH 221 3554 1004 HOH HOH B . 
HA 6 HOH 222 3555 1005 HOH HOH B . 
HA 6 HOH 223 3556 1006 HOH HOH B . 
HA 6 HOH 224 3557 1007 HOH HOH B . 
HA 6 HOH 225 3558 1008 HOH HOH B . 
HA 6 HOH 226 3559 1009 HOH HOH B . 
HA 6 HOH 227 3560 1010 HOH HOH B . 
HA 6 HOH 228 3561 1011 HOH HOH B . 
HA 6 HOH 229 3562 1012 HOH HOH B . 
HA 6 HOH 230 3563 1013 HOH HOH B . 
HA 6 HOH 231 3564 1015 HOH HOH B . 
HA 6 HOH 232 3565 1016 HOH HOH B . 
HA 6 HOH 233 3566 1018 HOH HOH B . 
HA 6 HOH 234 3567 1019 HOH HOH B . 
HA 6 HOH 235 3568 1020 HOH HOH B . 
HA 6 HOH 236 3569 1035 HOH HOH B . 
HA 6 HOH 237 3570 1069 HOH HOH B . 
HA 6 HOH 238 3571 1074 HOH HOH B . 
HA 6 HOH 239 3572 1076 HOH HOH B . 
HA 6 HOH 240 3573 1077 HOH HOH B . 
HA 6 HOH 241 3574 1078 HOH HOH B . 
HA 6 HOH 242 3575 1081 HOH HOH B . 
HA 6 HOH 243 3576 1124 HOH HOH B . 
HA 6 HOH 244 3577 1127 HOH HOH B . 
HA 6 HOH 245 3578 1128 HOH HOH B . 
HA 6 HOH 246 3579 1129 HOH HOH B . 
HA 6 HOH 247 3580 1130 HOH HOH B . 
HA 6 HOH 248 3581 1131 HOH HOH B . 
HA 6 HOH 249 3582 1132 HOH HOH B . 
HA 6 HOH 250 3583 1133 HOH HOH B . 
HA 6 HOH 251 3584 1134 HOH HOH B . 
HA 6 HOH 252 3585 1135 HOH HOH B . 
HA 6 HOH 253 3586 1136 HOH HOH B . 
HA 6 HOH 254 3587 1137 HOH HOH B . 
HA 6 HOH 255 3588 1138 HOH HOH B . 
HA 6 HOH 256 3589 1139 HOH HOH B . 
HA 6 HOH 257 3590 1140 HOH HOH B . 
HA 6 HOH 258 3591 1141 HOH HOH B . 
HA 6 HOH 259 3592 1142 HOH HOH B . 
HA 6 HOH 260 3593 1145 HOH HOH B . 
HA 6 HOH 261 3594 1146 HOH HOH B . 
HA 6 HOH 262 3595 1147 HOH HOH B . 
HA 6 HOH 263 3596 1148 HOH HOH B . 
HA 6 HOH 264 3597 1149 HOH HOH B . 
HA 6 HOH 265 3598 1150 HOH HOH B . 
HA 6 HOH 266 3599 1151 HOH HOH B . 
HA 6 HOH 267 3600 1161 HOH HOH B . 
HA 6 HOH 268 3601 1225 HOH HOH B . 
HA 6 HOH 269 3602 1243 HOH HOH B . 
HA 6 HOH 270 3603 1245 HOH HOH B . 
HA 6 HOH 271 3604 1246 HOH HOH B . 
HA 6 HOH 272 3605 1247 HOH HOH B . 
HA 6 HOH 273 3606 1248 HOH HOH B . 
IA 6 HOH 1   7778 4    HOH HOH C . 
IA 6 HOH 2   7779 40   HOH HOH C . 
IA 6 HOH 3   7780 44   HOH HOH C . 
IA 6 HOH 4   7781 53   HOH HOH C . 
IA 6 HOH 5   7782 60   HOH HOH C . 
IA 6 HOH 6   7783 61   HOH HOH C . 
IA 6 HOH 7   7784 63   HOH HOH C . 
IA 6 HOH 8   7785 72   HOH HOH C . 
IA 6 HOH 9   7786 76   HOH HOH C . 
IA 6 HOH 10  7787 83   HOH HOH C . 
IA 6 HOH 11  7788 85   HOH HOH C . 
IA 6 HOH 12  7789 86   HOH HOH C . 
IA 6 HOH 13  7790 88   HOH HOH C . 
IA 6 HOH 14  7791 93   HOH HOH C . 
IA 6 HOH 15  7792 112  HOH HOH C . 
IA 6 HOH 16  7793 131  HOH HOH C . 
IA 6 HOH 17  7794 140  HOH HOH C . 
IA 6 HOH 18  7795 150  HOH HOH C . 
IA 6 HOH 19  7796 157  HOH HOH C . 
IA 6 HOH 20  7797 161  HOH HOH C . 
IA 6 HOH 21  7798 168  HOH HOH C . 
IA 6 HOH 22  7799 183  HOH HOH C . 
IA 6 HOH 23  7800 194  HOH HOH C . 
IA 6 HOH 24  7801 201  HOH HOH C . 
IA 6 HOH 25  7802 207  HOH HOH C . 
IA 6 HOH 26  7803 217  HOH HOH C . 
IA 6 HOH 27  7804 225  HOH HOH C . 
IA 6 HOH 28  7805 226  HOH HOH C . 
IA 6 HOH 29  7806 241  HOH HOH C . 
IA 6 HOH 30  7807 242  HOH HOH C . 
IA 6 HOH 31  7808 244  HOH HOH C . 
IA 6 HOH 32  7809 245  HOH HOH C . 
IA 6 HOH 33  7810 247  HOH HOH C . 
IA 6 HOH 34  7811 252  HOH HOH C . 
IA 6 HOH 35  7812 257  HOH HOH C . 
IA 6 HOH 36  7813 258  HOH HOH C . 
IA 6 HOH 37  7814 264  HOH HOH C . 
IA 6 HOH 38  7815 273  HOH HOH C . 
IA 6 HOH 39  7816 276  HOH HOH C . 
IA 6 HOH 40  7817 279  HOH HOH C . 
IA 6 HOH 41  7818 291  HOH HOH C . 
IA 6 HOH 42  7819 301  HOH HOH C . 
IA 6 HOH 43  7820 307  HOH HOH C . 
IA 6 HOH 44  7821 308  HOH HOH C . 
IA 6 HOH 45  7822 309  HOH HOH C . 
IA 6 HOH 46  7823 311  HOH HOH C . 
IA 6 HOH 47  7824 314  HOH HOH C . 
IA 6 HOH 48  7825 326  HOH HOH C . 
IA 6 HOH 49  7826 327  HOH HOH C . 
IA 6 HOH 50  7827 339  HOH HOH C . 
IA 6 HOH 51  7828 340  HOH HOH C . 
IA 6 HOH 52  7829 345  HOH HOH C . 
IA 6 HOH 53  7830 355  HOH HOH C . 
IA 6 HOH 54  7831 362  HOH HOH C . 
IA 6 HOH 55  7832 370  HOH HOH C . 
IA 6 HOH 56  7833 371  HOH HOH C . 
IA 6 HOH 57  7834 372  HOH HOH C . 
IA 6 HOH 58  7835 377  HOH HOH C . 
IA 6 HOH 59  7836 380  HOH HOH C . 
IA 6 HOH 60  7837 384  HOH HOH C . 
IA 6 HOH 61  7838 386  HOH HOH C . 
IA 6 HOH 62  7839 468  HOH HOH C . 
IA 6 HOH 63  7840 471  HOH HOH C . 
IA 6 HOH 64  7841 474  HOH HOH C . 
IA 6 HOH 65  7842 476  HOH HOH C . 
IA 6 HOH 66  7843 477  HOH HOH C . 
IA 6 HOH 67  7844 478  HOH HOH C . 
IA 6 HOH 68  7845 479  HOH HOH C . 
IA 6 HOH 69  7846 481  HOH HOH C . 
IA 6 HOH 70  7847 483  HOH HOH C . 
IA 6 HOH 71  7848 484  HOH HOH C . 
IA 6 HOH 72  7849 486  HOH HOH C . 
IA 6 HOH 73  7850 487  HOH HOH C . 
IA 6 HOH 74  7851 488  HOH HOH C . 
IA 6 HOH 75  7852 489  HOH HOH C . 
IA 6 HOH 76  7853 490  HOH HOH C . 
IA 6 HOH 77  7854 491  HOH HOH C . 
IA 6 HOH 78  7855 492  HOH HOH C . 
IA 6 HOH 79  7856 493  HOH HOH C . 
IA 6 HOH 80  7857 494  HOH HOH C . 
IA 6 HOH 81  7858 495  HOH HOH C . 
IA 6 HOH 82  7859 499  HOH HOH C . 
IA 6 HOH 83  7860 500  HOH HOH C . 
IA 6 HOH 84  7861 502  HOH HOH C . 
IA 6 HOH 85  7862 509  HOH HOH C . 
IA 6 HOH 86  7863 510  HOH HOH C . 
IA 6 HOH 87  7864 512  HOH HOH C . 
IA 6 HOH 88  7865 513  HOH HOH C . 
IA 6 HOH 89  7866 514  HOH HOH C . 
IA 6 HOH 90  7867 520  HOH HOH C . 
IA 6 HOH 91  7868 521  HOH HOH C . 
IA 6 HOH 92  7869 522  HOH HOH C . 
IA 6 HOH 93  7870 524  HOH HOH C . 
IA 6 HOH 94  7871 525  HOH HOH C . 
IA 6 HOH 95  7872 526  HOH HOH C . 
IA 6 HOH 96  7873 527  HOH HOH C . 
IA 6 HOH 97  7874 531  HOH HOH C . 
IA 6 HOH 98  7875 559  HOH HOH C . 
IA 6 HOH 99  7876 560  HOH HOH C . 
IA 6 HOH 100 7877 561  HOH HOH C . 
IA 6 HOH 101 7878 623  HOH HOH C . 
IA 6 HOH 102 7879 624  HOH HOH C . 
IA 6 HOH 103 7880 659  HOH HOH C . 
IA 6 HOH 104 7881 704  HOH HOH C . 
IA 6 HOH 105 7882 706  HOH HOH C . 
IA 6 HOH 106 7883 707  HOH HOH C . 
IA 6 HOH 107 7884 709  HOH HOH C . 
IA 6 HOH 108 7885 746  HOH HOH C . 
IA 6 HOH 109 7886 749  HOH HOH C . 
IA 6 HOH 110 7887 754  HOH HOH C . 
IA 6 HOH 111 7888 758  HOH HOH C . 
IA 6 HOH 112 7889 760  HOH HOH C . 
IA 6 HOH 113 7890 761  HOH HOH C . 
IA 6 HOH 114 7891 762  HOH HOH C . 
IA 6 HOH 115 7892 763  HOH HOH C . 
IA 6 HOH 116 7893 774  HOH HOH C . 
IA 6 HOH 117 7894 776  HOH HOH C . 
IA 6 HOH 118 7895 779  HOH HOH C . 
IA 6 HOH 119 7896 782  HOH HOH C . 
IA 6 HOH 120 7897 792  HOH HOH C . 
IA 6 HOH 121 7898 793  HOH HOH C . 
IA 6 HOH 122 7899 795  HOH HOH C . 
IA 6 HOH 123 7900 796  HOH HOH C . 
IA 6 HOH 124 7901 797  HOH HOH C . 
IA 6 HOH 125 7902 798  HOH HOH C . 
IA 6 HOH 126 7903 799  HOH HOH C . 
IA 6 HOH 127 7904 800  HOH HOH C . 
IA 6 HOH 128 7905 801  HOH HOH C . 
IA 6 HOH 129 7906 802  HOH HOH C . 
IA 6 HOH 130 7907 803  HOH HOH C . 
IA 6 HOH 131 7908 804  HOH HOH C . 
IA 6 HOH 132 7909 805  HOH HOH C . 
IA 6 HOH 133 7910 806  HOH HOH C . 
IA 6 HOH 134 7911 807  HOH HOH C . 
IA 6 HOH 135 7912 808  HOH HOH C . 
IA 6 HOH 136 7913 809  HOH HOH C . 
IA 6 HOH 137 7914 810  HOH HOH C . 
IA 6 HOH 138 7915 811  HOH HOH C . 
IA 6 HOH 139 7916 820  HOH HOH C . 
IA 6 HOH 140 7917 821  HOH HOH C . 
IA 6 HOH 141 7918 822  HOH HOH C . 
IA 6 HOH 142 7919 823  HOH HOH C . 
IA 6 HOH 143 7920 826  HOH HOH C . 
IA 6 HOH 144 7921 827  HOH HOH C . 
IA 6 HOH 145 7922 829  HOH HOH C . 
IA 6 HOH 146 7923 830  HOH HOH C . 
IA 6 HOH 147 7924 832  HOH HOH C . 
IA 6 HOH 148 7925 833  HOH HOH C . 
IA 6 HOH 149 7926 834  HOH HOH C . 
IA 6 HOH 150 7927 835  HOH HOH C . 
IA 6 HOH 151 7928 836  HOH HOH C . 
IA 6 HOH 152 7929 838  HOH HOH C . 
IA 6 HOH 153 7930 840  HOH HOH C . 
IA 6 HOH 154 7931 841  HOH HOH C . 
IA 6 HOH 155 7932 842  HOH HOH C . 
IA 6 HOH 156 7933 843  HOH HOH C . 
IA 6 HOH 157 7934 844  HOH HOH C . 
IA 6 HOH 158 7935 845  HOH HOH C . 
IA 6 HOH 159 7936 846  HOH HOH C . 
IA 6 HOH 160 7937 847  HOH HOH C . 
IA 6 HOH 161 7938 848  HOH HOH C . 
IA 6 HOH 162 7939 849  HOH HOH C . 
IA 6 HOH 163 7940 850  HOH HOH C . 
IA 6 HOH 164 7941 851  HOH HOH C . 
IA 6 HOH 165 7942 852  HOH HOH C . 
IA 6 HOH 166 7943 853  HOH HOH C . 
IA 6 HOH 167 7944 854  HOH HOH C . 
IA 6 HOH 168 7945 859  HOH HOH C . 
IA 6 HOH 169 7946 860  HOH HOH C . 
IA 6 HOH 170 7947 861  HOH HOH C . 
IA 6 HOH 171 7948 862  HOH HOH C . 
IA 6 HOH 172 7949 863  HOH HOH C . 
IA 6 HOH 173 7950 867  HOH HOH C . 
IA 6 HOH 174 7951 868  HOH HOH C . 
IA 6 HOH 175 7952 869  HOH HOH C . 
IA 6 HOH 176 7953 870  HOH HOH C . 
IA 6 HOH 177 7954 871  HOH HOH C . 
IA 6 HOH 178 7955 872  HOH HOH C . 
IA 6 HOH 179 7956 873  HOH HOH C . 
IA 6 HOH 180 7957 874  HOH HOH C . 
IA 6 HOH 181 7958 875  HOH HOH C . 
IA 6 HOH 182 7959 876  HOH HOH C . 
IA 6 HOH 183 7960 877  HOH HOH C . 
IA 6 HOH 184 7961 956  HOH HOH C . 
IA 6 HOH 185 7962 1021 HOH HOH C . 
IA 6 HOH 186 7963 1022 HOH HOH C . 
IA 6 HOH 187 7964 1023 HOH HOH C . 
IA 6 HOH 188 7965 1024 HOH HOH C . 
IA 6 HOH 189 7966 1025 HOH HOH C . 
IA 6 HOH 190 7967 1027 HOH HOH C . 
IA 6 HOH 191 7968 1028 HOH HOH C . 
IA 6 HOH 192 7969 1029 HOH HOH C . 
IA 6 HOH 193 7970 1030 HOH HOH C . 
IA 6 HOH 194 7971 1031 HOH HOH C . 
IA 6 HOH 195 7972 1032 HOH HOH C . 
IA 6 HOH 196 7973 1033 HOH HOH C . 
IA 6 HOH 197 7974 1034 HOH HOH C . 
IA 6 HOH 198 7975 1036 HOH HOH C . 
IA 6 HOH 199 7976 1037 HOH HOH C . 
IA 6 HOH 200 7977 1038 HOH HOH C . 
IA 6 HOH 201 7978 1039 HOH HOH C . 
IA 6 HOH 202 7979 1042 HOH HOH C . 
IA 6 HOH 203 7980 1075 HOH HOH C . 
IA 6 HOH 204 7981 1082 HOH HOH C . 
IA 6 HOH 205 7982 1083 HOH HOH C . 
IA 6 HOH 206 7983 1084 HOH HOH C . 
IA 6 HOH 207 7984 1085 HOH HOH C . 
IA 6 HOH 208 7985 1086 HOH HOH C . 
IA 6 HOH 209 7986 1087 HOH HOH C . 
IA 6 HOH 210 7987 1088 HOH HOH C . 
IA 6 HOH 211 7988 1089 HOH HOH C . 
IA 6 HOH 212 7989 1090 HOH HOH C . 
IA 6 HOH 213 7990 1091 HOH HOH C . 
IA 6 HOH 214 7991 1144 HOH HOH C . 
IA 6 HOH 215 7992 1152 HOH HOH C . 
IA 6 HOH 216 7993 1153 HOH HOH C . 
IA 6 HOH 217 7994 1154 HOH HOH C . 
IA 6 HOH 218 7995 1155 HOH HOH C . 
IA 6 HOH 219 7996 1156 HOH HOH C . 
IA 6 HOH 220 7997 1157 HOH HOH C . 
IA 6 HOH 221 7998 1158 HOH HOH C . 
IA 6 HOH 222 7999 1159 HOH HOH C . 
IA 6 HOH 223 8000 1160 HOH HOH C . 
IA 6 HOH 224 8001 1162 HOH HOH C . 
IA 6 HOH 225 8002 1163 HOH HOH C . 
IA 6 HOH 226 8003 1164 HOH HOH C . 
IA 6 HOH 227 8004 1165 HOH HOH C . 
IA 6 HOH 228 8005 1166 HOH HOH C . 
IA 6 HOH 229 8006 1168 HOH HOH C . 
IA 6 HOH 230 8007 1169 HOH HOH C . 
IA 6 HOH 231 8008 1171 HOH HOH C . 
IA 6 HOH 232 8009 1173 HOH HOH C . 
IA 6 HOH 233 8010 1174 HOH HOH C . 
IA 6 HOH 234 8011 1175 HOH HOH C . 
IA 6 HOH 235 8012 1218 HOH HOH C . 
IA 6 HOH 236 8013 1219 HOH HOH C . 
IA 6 HOH 237 8014 1220 HOH HOH C . 
IA 6 HOH 238 8015 1221 HOH HOH C . 
IA 6 HOH 239 8016 1222 HOH HOH C . 
IA 6 HOH 240 8017 1224 HOH HOH C . 
IA 6 HOH 241 8018 1226 HOH HOH C . 
IA 6 HOH 242 8019 1249 HOH HOH C . 
IA 6 HOH 243 8020 1253 HOH HOH C . 
IA 6 HOH 244 8021 1254 HOH HOH C . 
IA 6 HOH 245 8022 1255 HOH HOH C . 
IA 6 HOH 246 8023 1256 HOH HOH C . 
IA 6 HOH 247 8024 1257 HOH HOH C . 
IA 6 HOH 248 8025 1258 HOH HOH C . 
IA 6 HOH 249 8026 1259 HOH HOH C . 
IA 6 HOH 250 8027 1260 HOH HOH C . 
IA 6 HOH 251 8028 1261 HOH HOH C . 
IA 6 HOH 252 8029 1263 HOH HOH C . 
JA 6 HOH 1   1000 2    HOH HOH D . 
JA 6 HOH 2   1001 3    HOH HOH D . 
JA 6 HOH 3   1002 5    HOH HOH D . 
JA 6 HOH 4   1003 6    HOH HOH D . 
JA 6 HOH 5   1004 9    HOH HOH D . 
JA 6 HOH 6   1005 11   HOH HOH D . 
JA 6 HOH 7   1006 14   HOH HOH D . 
JA 6 HOH 8   1007 15   HOH HOH D . 
JA 6 HOH 9   1008 16   HOH HOH D . 
JA 6 HOH 10  1009 17   HOH HOH D . 
JA 6 HOH 11  1010 23   HOH HOH D . 
JA 6 HOH 12  1011 26   HOH HOH D . 
JA 6 HOH 13  1012 28   HOH HOH D . 
JA 6 HOH 14  1013 31   HOH HOH D . 
JA 6 HOH 15  1014 33   HOH HOH D . 
JA 6 HOH 16  1015 37   HOH HOH D . 
JA 6 HOH 17  1016 39   HOH HOH D . 
JA 6 HOH 18  1017 41   HOH HOH D . 
JA 6 HOH 19  1018 46   HOH HOH D . 
JA 6 HOH 20  1019 47   HOH HOH D . 
JA 6 HOH 21  1020 49   HOH HOH D . 
JA 6 HOH 22  1021 51   HOH HOH D . 
JA 6 HOH 23  1022 64   HOH HOH D . 
JA 6 HOH 24  1023 66   HOH HOH D . 
JA 6 HOH 25  1024 69   HOH HOH D . 
JA 6 HOH 26  1025 79   HOH HOH D . 
JA 6 HOH 27  1026 80   HOH HOH D . 
JA 6 HOH 28  1027 81   HOH HOH D . 
JA 6 HOH 29  1028 82   HOH HOH D . 
JA 6 HOH 30  1029 90   HOH HOH D . 
JA 6 HOH 31  1030 91   HOH HOH D . 
JA 6 HOH 32  1031 92   HOH HOH D . 
JA 6 HOH 33  1032 94   HOH HOH D . 
JA 6 HOH 34  1033 95   HOH HOH D . 
JA 6 HOH 35  1034 96   HOH HOH D . 
JA 6 HOH 36  1035 97   HOH HOH D . 
JA 6 HOH 37  1036 98   HOH HOH D . 
JA 6 HOH 38  1037 100  HOH HOH D . 
JA 6 HOH 39  1038 101  HOH HOH D . 
JA 6 HOH 40  1039 104  HOH HOH D . 
JA 6 HOH 41  1040 105  HOH HOH D . 
JA 6 HOH 42  1041 106  HOH HOH D . 
JA 6 HOH 43  1042 108  HOH HOH D . 
JA 6 HOH 44  1043 113  HOH HOH D . 
JA 6 HOH 45  1044 114  HOH HOH D . 
JA 6 HOH 46  1045 115  HOH HOH D . 
JA 6 HOH 47  1046 117  HOH HOH D . 
JA 6 HOH 48  1047 118  HOH HOH D . 
JA 6 HOH 49  1048 120  HOH HOH D . 
JA 6 HOH 50  1049 121  HOH HOH D . 
JA 6 HOH 51  1050 122  HOH HOH D . 
JA 6 HOH 52  1051 125  HOH HOH D . 
JA 6 HOH 53  1052 126  HOH HOH D . 
JA 6 HOH 54  1053 139  HOH HOH D . 
JA 6 HOH 55  1054 142  HOH HOH D . 
JA 6 HOH 56  1055 148  HOH HOH D . 
JA 6 HOH 57  1056 149  HOH HOH D . 
JA 6 HOH 58  1057 152  HOH HOH D . 
JA 6 HOH 59  1058 154  HOH HOH D . 
JA 6 HOH 60  1059 155  HOH HOH D . 
JA 6 HOH 61  1060 162  HOH HOH D . 
JA 6 HOH 62  1061 163  HOH HOH D . 
JA 6 HOH 63  1062 165  HOH HOH D . 
JA 6 HOH 64  1063 169  HOH HOH D . 
JA 6 HOH 65  1064 171  HOH HOH D . 
JA 6 HOH 66  1065 172  HOH HOH D . 
JA 6 HOH 67  1066 174  HOH HOH D . 
JA 6 HOH 68  1067 180  HOH HOH D . 
JA 6 HOH 69  1068 181  HOH HOH D . 
JA 6 HOH 70  1069 182  HOH HOH D . 
JA 6 HOH 71  1070 188  HOH HOH D . 
JA 6 HOH 72  1071 190  HOH HOH D . 
JA 6 HOH 73  1072 191  HOH HOH D . 
JA 6 HOH 74  1073 192  HOH HOH D . 
JA 6 HOH 75  1074 193  HOH HOH D . 
JA 6 HOH 76  1075 195  HOH HOH D . 
JA 6 HOH 77  1076 204  HOH HOH D . 
JA 6 HOH 78  1077 210  HOH HOH D . 
JA 6 HOH 79  1078 211  HOH HOH D . 
JA 6 HOH 80  1079 214  HOH HOH D . 
JA 6 HOH 81  1080 215  HOH HOH D . 
JA 6 HOH 82  1081 218  HOH HOH D . 
JA 6 HOH 83  1082 219  HOH HOH D . 
JA 6 HOH 84  1083 220  HOH HOH D . 
JA 6 HOH 85  1084 228  HOH HOH D . 
JA 6 HOH 86  1085 232  HOH HOH D . 
JA 6 HOH 87  1086 239  HOH HOH D . 
JA 6 HOH 88  1087 240  HOH HOH D . 
JA 6 HOH 89  1088 246  HOH HOH D . 
JA 6 HOH 90  1089 249  HOH HOH D . 
JA 6 HOH 91  1090 250  HOH HOH D . 
JA 6 HOH 92  1091 254  HOH HOH D . 
JA 6 HOH 93  1092 256  HOH HOH D . 
JA 6 HOH 94  1093 265  HOH HOH D . 
JA 6 HOH 95  1094 269  HOH HOH D . 
JA 6 HOH 96  1095 277  HOH HOH D . 
JA 6 HOH 97  1096 283  HOH HOH D . 
JA 6 HOH 98  1097 285  HOH HOH D . 
JA 6 HOH 99  1098 286  HOH HOH D . 
JA 6 HOH 100 1099 288  HOH HOH D . 
JA 6 HOH 101 1100 292  HOH HOH D . 
JA 6 HOH 102 1101 296  HOH HOH D . 
JA 6 HOH 103 1102 297  HOH HOH D . 
JA 6 HOH 104 1103 318  HOH HOH D . 
JA 6 HOH 105 1104 319  HOH HOH D . 
JA 6 HOH 106 1105 321  HOH HOH D . 
JA 6 HOH 107 1106 331  HOH HOH D . 
JA 6 HOH 108 1107 337  HOH HOH D . 
JA 6 HOH 109 1108 338  HOH HOH D . 
JA 6 HOH 110 1109 341  HOH HOH D . 
JA 6 HOH 111 1110 342  HOH HOH D . 
JA 6 HOH 112 1111 344  HOH HOH D . 
JA 6 HOH 113 1112 348  HOH HOH D . 
JA 6 HOH 114 1113 352  HOH HOH D . 
JA 6 HOH 115 1114 353  HOH HOH D . 
JA 6 HOH 116 1115 356  HOH HOH D . 
JA 6 HOH 117 1116 359  HOH HOH D . 
JA 6 HOH 118 1117 364  HOH HOH D . 
JA 6 HOH 119 1118 366  HOH HOH D . 
JA 6 HOH 120 1119 367  HOH HOH D . 
JA 6 HOH 121 1120 381  HOH HOH D . 
JA 6 HOH 122 1121 480  HOH HOH D . 
JA 6 HOH 123 1122 506  HOH HOH D . 
JA 6 HOH 124 1123 507  HOH HOH D . 
JA 6 HOH 125 1124 532  HOH HOH D . 
JA 6 HOH 126 1125 533  HOH HOH D . 
JA 6 HOH 127 1126 535  HOH HOH D . 
JA 6 HOH 128 1127 536  HOH HOH D . 
JA 6 HOH 129 1128 551  HOH HOH D . 
JA 6 HOH 130 1129 552  HOH HOH D . 
JA 6 HOH 131 1130 553  HOH HOH D . 
JA 6 HOH 132 1131 554  HOH HOH D . 
JA 6 HOH 133 1132 555  HOH HOH D . 
JA 6 HOH 134 1133 556  HOH HOH D . 
JA 6 HOH 135 1134 557  HOH HOH D . 
JA 6 HOH 136 1135 587  HOH HOH D . 
JA 6 HOH 137 1136 593  HOH HOH D . 
JA 6 HOH 138 1137 595  HOH HOH D . 
JA 6 HOH 139 1138 615  HOH HOH D . 
JA 6 HOH 140 1139 616  HOH HOH D . 
JA 6 HOH 141 1140 619  HOH HOH D . 
JA 6 HOH 142 1141 636  HOH HOH D . 
JA 6 HOH 143 1142 640  HOH HOH D . 
JA 6 HOH 144 1143 641  HOH HOH D . 
JA 6 HOH 145 1144 644  HOH HOH D . 
JA 6 HOH 146 1145 657  HOH HOH D . 
JA 6 HOH 147 1146 658  HOH HOH D . 
JA 6 HOH 148 1147 770  HOH HOH D . 
JA 6 HOH 149 1148 837  HOH HOH D . 
JA 6 HOH 150 1149 839  HOH HOH D . 
JA 6 HOH 151 1150 855  HOH HOH D . 
JA 6 HOH 152 1151 856  HOH HOH D . 
JA 6 HOH 153 1152 857  HOH HOH D . 
JA 6 HOH 154 1153 858  HOH HOH D . 
JA 6 HOH 155 1154 864  HOH HOH D . 
JA 6 HOH 156 1155 865  HOH HOH D . 
JA 6 HOH 157 1156 866  HOH HOH D . 
JA 6 HOH 158 1157 881  HOH HOH D . 
JA 6 HOH 159 1158 882  HOH HOH D . 
JA 6 HOH 160 1159 883  HOH HOH D . 
JA 6 HOH 161 1160 884  HOH HOH D . 
JA 6 HOH 162 1161 885  HOH HOH D . 
JA 6 HOH 163 1162 886  HOH HOH D . 
JA 6 HOH 164 1163 887  HOH HOH D . 
JA 6 HOH 165 1164 889  HOH HOH D . 
JA 6 HOH 166 1165 890  HOH HOH D . 
JA 6 HOH 167 1166 891  HOH HOH D . 
JA 6 HOH 168 1167 892  HOH HOH D . 
JA 6 HOH 169 1168 893  HOH HOH D . 
JA 6 HOH 170 1169 894  HOH HOH D . 
JA 6 HOH 171 1170 895  HOH HOH D . 
JA 6 HOH 172 1171 897  HOH HOH D . 
JA 6 HOH 173 1172 898  HOH HOH D . 
JA 6 HOH 174 1173 900  HOH HOH D . 
JA 6 HOH 175 1174 901  HOH HOH D . 
JA 6 HOH 176 1175 902  HOH HOH D . 
JA 6 HOH 177 1176 903  HOH HOH D . 
JA 6 HOH 178 1177 904  HOH HOH D . 
JA 6 HOH 179 1178 905  HOH HOH D . 
JA 6 HOH 180 1179 906  HOH HOH D . 
JA 6 HOH 181 1180 907  HOH HOH D . 
JA 6 HOH 182 1181 908  HOH HOH D . 
JA 6 HOH 183 1182 909  HOH HOH D . 
JA 6 HOH 184 1183 910  HOH HOH D . 
JA 6 HOH 185 1184 911  HOH HOH D . 
JA 6 HOH 186 1185 912  HOH HOH D . 
JA 6 HOH 187 1186 913  HOH HOH D . 
JA 6 HOH 188 1187 914  HOH HOH D . 
JA 6 HOH 189 1188 915  HOH HOH D . 
JA 6 HOH 190 1189 916  HOH HOH D . 
JA 6 HOH 191 1190 919  HOH HOH D . 
JA 6 HOH 192 1191 921  HOH HOH D . 
JA 6 HOH 193 1192 922  HOH HOH D . 
JA 6 HOH 194 1193 923  HOH HOH D . 
JA 6 HOH 195 1194 924  HOH HOH D . 
JA 6 HOH 196 1195 925  HOH HOH D . 
JA 6 HOH 197 1196 926  HOH HOH D . 
JA 6 HOH 198 1197 927  HOH HOH D . 
JA 6 HOH 199 1198 928  HOH HOH D . 
JA 6 HOH 200 1199 929  HOH HOH D . 
JA 6 HOH 201 1200 930  HOH HOH D . 
JA 6 HOH 202 1201 948  HOH HOH D . 
JA 6 HOH 203 1202 953  HOH HOH D . 
JA 6 HOH 204 1203 954  HOH HOH D . 
JA 6 HOH 205 1204 958  HOH HOH D . 
JA 6 HOH 206 1205 968  HOH HOH D . 
JA 6 HOH 207 1206 980  HOH HOH D . 
JA 6 HOH 208 1207 993  HOH HOH D . 
JA 6 HOH 209 1208 995  HOH HOH D . 
JA 6 HOH 210 1209 996  HOH HOH D . 
JA 6 HOH 211 1210 1040 HOH HOH D . 
JA 6 HOH 212 1211 1041 HOH HOH D . 
JA 6 HOH 213 1212 1044 HOH HOH D . 
JA 6 HOH 214 1213 1045 HOH HOH D . 
JA 6 HOH 215 1214 1046 HOH HOH D . 
JA 6 HOH 216 1215 1047 HOH HOH D . 
JA 6 HOH 217 1216 1048 HOH HOH D . 
JA 6 HOH 218 1217 1049 HOH HOH D . 
JA 6 HOH 219 1218 1051 HOH HOH D . 
JA 6 HOH 220 1219 1052 HOH HOH D . 
JA 6 HOH 221 1220 1053 HOH HOH D . 
JA 6 HOH 222 1221 1054 HOH HOH D . 
JA 6 HOH 223 1222 1055 HOH HOH D . 
JA 6 HOH 224 1223 1056 HOH HOH D . 
JA 6 HOH 225 1224 1057 HOH HOH D . 
JA 6 HOH 226 1225 1058 HOH HOH D . 
JA 6 HOH 227 1226 1059 HOH HOH D . 
JA 6 HOH 228 1227 1060 HOH HOH D . 
JA 6 HOH 229 1228 1061 HOH HOH D . 
JA 6 HOH 230 1229 1062 HOH HOH D . 
JA 6 HOH 231 1230 1063 HOH HOH D . 
JA 6 HOH 232 1231 1067 HOH HOH D . 
JA 6 HOH 233 1232 1072 HOH HOH D . 
JA 6 HOH 234 1233 1092 HOH HOH D . 
JA 6 HOH 235 1234 1093 HOH HOH D . 
JA 6 HOH 236 1235 1094 HOH HOH D . 
JA 6 HOH 237 1236 1096 HOH HOH D . 
JA 6 HOH 238 1237 1099 HOH HOH D . 
JA 6 HOH 239 1238 1113 HOH HOH D . 
JA 6 HOH 240 1239 1122 HOH HOH D . 
JA 6 HOH 241 1240 1143 HOH HOH D . 
JA 6 HOH 242 1241 1167 HOH HOH D . 
JA 6 HOH 243 1242 1170 HOH HOH D . 
JA 6 HOH 244 1243 1172 HOH HOH D . 
JA 6 HOH 245 1244 1176 HOH HOH D . 
JA 6 HOH 246 1245 1177 HOH HOH D . 
JA 6 HOH 247 1246 1178 HOH HOH D . 
JA 6 HOH 248 1247 1179 HOH HOH D . 
JA 6 HOH 249 1248 1180 HOH HOH D . 
JA 6 HOH 250 1249 1181 HOH HOH D . 
JA 6 HOH 251 1250 1182 HOH HOH D . 
JA 6 HOH 252 1251 1183 HOH HOH D . 
JA 6 HOH 253 1252 1184 HOH HOH D . 
JA 6 HOH 254 1253 1185 HOH HOH D . 
JA 6 HOH 255 1254 1186 HOH HOH D . 
JA 6 HOH 256 1255 1187 HOH HOH D . 
JA 6 HOH 257 1256 1188 HOH HOH D . 
JA 6 HOH 258 1257 1189 HOH HOH D . 
JA 6 HOH 259 1258 1190 HOH HOH D . 
JA 6 HOH 260 1259 1191 HOH HOH D . 
JA 6 HOH 261 1260 1193 HOH HOH D . 
JA 6 HOH 262 1261 1194 HOH HOH D . 
JA 6 HOH 263 1262 1197 HOH HOH D . 
JA 6 HOH 264 1263 1198 HOH HOH D . 
JA 6 HOH 265 1264 1199 HOH HOH D . 
JA 6 HOH 266 1265 1200 HOH HOH D . 
JA 6 HOH 267 1266 1201 HOH HOH D . 
JA 6 HOH 268 1267 1202 HOH HOH D . 
JA 6 HOH 269 1268 1203 HOH HOH D . 
JA 6 HOH 270 1269 1204 HOH HOH D . 
JA 6 HOH 271 1270 1205 HOH HOH D . 
JA 6 HOH 272 1271 1206 HOH HOH D . 
JA 6 HOH 273 1272 1207 HOH HOH D . 
JA 6 HOH 274 1273 1208 HOH HOH D . 
JA 6 HOH 275 1274 1209 HOH HOH D . 
JA 6 HOH 276 1275 1210 HOH HOH D . 
JA 6 HOH 277 1276 1211 HOH HOH D . 
JA 6 HOH 278 1277 1212 HOH HOH D . 
JA 6 HOH 279 1278 1213 HOH HOH D . 
JA 6 HOH 280 1279 1214 HOH HOH D . 
JA 6 HOH 281 1280 1227 HOH HOH D . 
JA 6 HOH 282 1281 1228 HOH HOH D . 
JA 6 HOH 283 1282 1229 HOH HOH D . 
JA 6 HOH 284 1283 1230 HOH HOH D . 
JA 6 HOH 285 1284 1231 HOH HOH D . 
JA 6 HOH 286 1285 1232 HOH HOH D . 
JA 6 HOH 287 1286 1234 HOH HOH D . 
JA 6 HOH 288 1287 1235 HOH HOH D . 
JA 6 HOH 289 1288 1236 HOH HOH D . 
JA 6 HOH 290 1289 1262 HOH HOH D . 
JA 6 HOH 291 1290 1264 HOH HOH D . 
JA 6 HOH 292 1291 1265 HOH HOH D . 
JA 6 HOH 293 1292 1266 HOH HOH D . 
JA 6 HOH 294 1293 1267 HOH HOH D . 
JA 6 HOH 295 1294 1268 HOH HOH D . 
JA 6 HOH 296 1295 1269 HOH HOH D . 
JA 6 HOH 297 1296 1270 HOH HOH D . 
JA 6 HOH 298 1297 1271 HOH HOH D . 
JA 6 HOH 299 1298 1272 HOH HOH D . 
JA 6 HOH 300 1299 1273 HOH HOH D . 
JA 6 HOH 301 1300 1274 HOH HOH D . 
JA 6 HOH 302 1301 1275 HOH HOH D . 
JA 6 HOH 303 1302 1276 HOH HOH D . 
# 
